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We present a detailed study on the temperature-dependent THz spectra of the polycrystalline amino acids, L-serine and L-cysteine, for wavenumbers from 20 to 120 cm−1 and temperatures from 4 to 300 K. Even though the structure of these two amino acids is very similar, with a sulfur atom in the side chain of cysteine instead of an oxygen atom in serine, the excitation spectra are drastically different. Obviously, the vibrational dynamics strongly depend on the ability of cysteine to form sulfur–hydrogen bonds. In addition, cysteine undergoes an order–disorder type phase transition close to 80 K, documented by additional specific heat experiments, with accompanying anomalies in the THz results. On increasing temperatures, well-defined vibrational excitations exhibit significant shifts in the eigenfrequencies with concomitant line-broadening yielding partly overlapping modes. Interestingly, several modes completely lose all their dipolar strength and are unobservable under ambient conditions. Comparing the recent results to the published work utilizing THz, Raman, and neutron-scattering techniques, as well as with ab initio simulations, we aim at a consistent analysis of the results ascribing certain eigenfrequencies to distinct collective lattice modes. We document that THz spectra can be used to fine-tune the parameters of model calculations and as fingerprint properties of certain amino acids. In addition, we analyzed the low-temperature heat capacity of both the compounds and detected strong excess contributions compared to the canonical Debye behavior of crystalline solids, indicating soft excitations and a strongly enhanced phonon-density of states at low frequencies. [ABSTRACT FROM AUTHOR]

Finding low-energy structures of ligand-protected clusters is challenging due to the enormous conformational space and the high computational cost of accurate quantum chemical methods for determining the structures and energies of conformers. Here, we adopted and utilized a kernel rigid regression based machine learning method to accelerate the search for low-energy structures of ligand-protected clusters. We chose the Au25(Cys)18 (Cys: cysteine) cluster as a model system to test and demonstrate our method. We found that the low-energy structures of the cluster are characterized by a specific hydrogen bond type in the cysteine. The different configurations of the ligand layer influence the structural and electronic properties of clusters. [ABSTRACT FROM AUTHOR]

Redox reactions, involving electron transfer, are critical to human physiology. However, progress in understanding redox metabolism is hindered by flawed analytical methods. This review highlights emerging techniques that promise to revolutionize redox research, enhancing our comprehension of human health and disease. Oxygen, vital for aerobic metabolism, also produces reactive oxygen species (ROS), such as superoxide and hydrogen peroxide. While historically seen as harmful, ROS at low concentrations are now recognized as key regulators of cell signaling. A balance between ROS and antioxidants, known as redox balance, is crucial, and deviations can lead to oxidative stress. Recent studies have distinguished beneficial "oxidative eustress" from harmful "oxidative distress." New techniques, such as advanced mass spectrometry and high‐throughput immunoassays, offer improved accuracy in measuring redox states and oxidative damage. These advancements are pivotal for understanding redox signaling, cysteine oxidation, and their implications for disease. Looking ahead, the development of precision redox medicine could lead to better treatments for oxidative stress‐related diseases and foster interventions promoting health. [ABSTRACT FROM AUTHOR]

The quest for novel chromophoric materials with tunable properties to match the natural spectrum of skin tones lacks comprehensive solutions, particularly in harnessing natural proteins for pigment synthesis. This research delved into the synthesis of sub‐micron Keratin‐Cysteine particles inspired by natural pigment production pathways. Adjustment of the initial conditions of the water‐based reaction between keratin, tyrosinase and cysteine, yielded Keratin‐Cysteine particles with colors tunable within the light to intermediate skin tone range. A systematic investigation of the reaction conditions through factorial design of experiment (DOE) identified the sequence of addition of tyrosinase and cysteine as the key determinant of color tone. Ultraviolet‐visible (UV‐Vis) spectroscopy, attenuated total reflectance Fourier transform infrared (ATR‐FTIR) spectroscopy and color analysis were performed to elucidate the reaction mechanism. This research presents a promising approach to chromophore synthesis for cosmetic and biomedical applications. [ABSTRACT FROM AUTHOR]

A novel approach for reducing mercury content in fish meat during post‐packaging storage is developed to extend the margin of their safe consumption. It involves employing a single‐component aqueous medium containing cysteine, as the active agent responsible for displacing mercury from fish proteins and its stabilization in the medium without the need for pH adjustments. The mercury removal efficiency depends on the cysteine concentration and its ratio to fish muscle. Using 1.2 wt% cysteine enables a reduction of mercury in canned Albacore tuna by 25–35%, depending on the fish product type and the exposure time of up to 2 weeks. The potential for the successful application of the developed method in active food packaging solutions is studied for the simultaneous or subsequent purification of the extraction solution through adsorption. Using thiolated silica could potentially enable the extraction process but it is shown that the presence of cysteine significantly hinders the adsorption. [ABSTRACT FROM AUTHOR]

Breast cancer is the most prevalent neoplasm affecting women globally, of which a notable proportion of cases are triple-negative breast cancer (TNBC). However, there are limited curative treatment options for patients with TNBC, despite advancements in the field. Amino acids and amino acid transporters serve vital roles in the regulation of tumor metabolism. Notably, cystine and cysteine can interconvert via a redox reaction, with cysteine exerting control on cell survival and growth and exogenous cystine serving a crucial role in the proliferation of numerous types of cancers. Breast cancer has been reported to disrupt the cystine/cysteine metabolism pathway, as cystine and cysteine transporters affect the development and growth of tumors. The present review aims to provide a comprehensive overview of the metabolic pathways involving cystine and cysteine in normal and TNBC cells. Furthermore, the roles of cystine and cysteine transporters in TNBC progression and metastasis and their potential as therapeutic targets for treatment of TNBC are evaluated. [ABSTRACT FROM AUTHOR]

Ferroptosis is a cell death modality in which iron-dependent lipid peroxides accumulate on cell membranes. Cysteine, a limiting substrate for the glutathione system that neutralizes lipid peroxidation and prevents ferroptosis, can be converted by cystine reduction or synthesized from methionine. However, accumulating evidence shows methionine-based cysteine synthesis fails to effectively rescue intracellular cysteine levels upon cystine deprivation and is unable to inhibit ferroptosis. Here, we report that methionine-based cysteine synthesis is tissue-specific. Unexpectedly, we find that rather than inhibiting ferroptosis, methionine in fact plays an essential role during cystine deprivation-induced ferroptosis. Methionine-derived S-adenosylmethionine (SAM) contributes to methylation-dependent ubiquinone synthesis, which leads to lipid peroxides accumulation and subsequent ferroptosis. Moreover, SAM supplementation synergizes with Imidazole Ketone Erastin in a tumor growth suppression mouse model. Inhibiting the enzyme that converts methionine to SAM protects heart tissue from Doxorubicin-induced and ferroptosis-driven cardiomyopathy. This study broadens our understanding about the intersection of amino acid metabolism and ferroptosis regulation, providing insight into the underlying mechanisms and suggesting the methionine-SAM axis is a promising therapeutic strategy to treat ferroptosis-related diseases. Ferroptosis is regulated by amino acid metabolism. Here, authors show that the methionine-SAM-UQ axis is responsible for mtROS generation and ferroptosis induction, suggesting potential therapeutic strategies for diseases associated with ferroptosis. [ABSTRACT FROM AUTHOR]

Cystathionine γ-lyase (CTH) is a critical enzyme in the reverse transsulfuration pathway, the major route for the metabolism of sulfur-containing amino acids, notably converting cystathionine to cysteine. We reported that CTH supports gastritis induced by the pathogen Helicobacter pylori. Herein our aim was to investigate the role of CTH in colonic inflammation. First, we found that CTH is induced in the colon mucosa in mice with dextran sulfate sodium-induced colitis. Expression of CTH was completely absent in the colon of Cth–/– mice. We observed that clinical and histological parameters are ameliorated in Cth-deficient mice compared to wild-type animals. However, Cth deletion had no effect on tumorigenesis and the level of dysplasia in mice treated with azoxymethane-DSS, as a reliable model of colitis-associated carcinogenesis. Mechanistically, we determined that the deletion of the gene Slc7a11 encoding for solute carrier family 7 member 11, the transporter of the anionic form of cysteine, does not affect DSS colitis. Lastly, we found that the richness and diversity of the fecal microbiota were significantly increased in Cth–/– mice compared to both WT and Slc7a11–/– mice. In conclusion, our data suggest that the enzyme CTH represents a target for clinical intervention in patients with inflammatory bowel disease, potentially by beneficially reshaping the composition of the gut microbiota. [ABSTRACT FROM AUTHOR]

The report presents first high performance liquid chromatography-tandem mass spectrometry (HPLC-MS/MS) based method for the determination of plasma 2-(3-hydroxy-5-phosphonooxymethyl-2-methyl-4-pyridyl)-1,3-thiazolidine-4-carboxylic acid (HPPTCA), an adduct of cysteine and active form of vitamin B6 pyridoxal 5′-phosphate. The assay employs 4-deoxypyridoxine (4-DPD) as an internal standard. Sample preparation procedure primarily involves acetonitrile (ACN) extraction of HPPTCA from plasma proteins, sample deproteinization by ultrafiltration, and dilution of ultrafiltrate with mobile phase prior to chromatographic analysis. The chromatographic separations of HPPTCA and 4-DPD are achieved within 6 min at 20 °C on X-Bridge Glycan BEH Amide (100 × 2.1 mm, 2.5 μm) column using gradient elution. The eluent consists of 0.1% formic acid in a mixture of solvent A (water and ACN (95:5, v: v)) and solvent B (water and ACN (5:95, v: v)) delivered at a flow rate of 0.3 mL/min. The assay linearity was observed within 0.25-10 µmol/L in plasma. The limit of quantification was found to be 0.25 µmol/L. The method was successfully applied to plasma samples delivered by apparently healthy donors showing that the HPLC-MS/MS assay is suitable for human plasma screening. The presence of HPPTCA was confirmed in eleven of fifteen study samples. The HPPTCA concentration ranged from 0.55 to 8.39 µmol/L. [ABSTRACT FROM AUTHOR]

This paper reported an ultrafast solvent- and metal-free method of constructing disulfide bonds (–S–S–) by oxidative homo- and cross-coupling of thiols with BrCCl3 and DIPEA. This fast reaction successfully synthesized unsymmetric disulfides with high yields of up to 99% from benzylic, aryl and aliphatic thiols, without strong oxidant, metal-based reagents and catalysts. This direct disulfuration strategy was also applied to efficiently form symmetric disulfides. Our method was further capable of modifying or protecting cysteine derivatives and preparing protein inhibitors. This work provides a simple and efficient approach for constructing disulfide-containing compounds. [ABSTRACT FROM AUTHOR]

This work reported gold nanoparticles (AuNPs)-based colorimetric immunoassay with the Cu-based metal–organic framework (MOF) to load pyrroloquinoline quinone (PQQ) for the catalytic oxidation of cysteine. In this method, both Cu2+ and PQQ in the MOF could promote the oxidation of inducer cysteine by redox cycling, thus limiting the cysteine-induced aggregation of AuNPs and achieving dual signal amplification. Specifically, the recombinant carcinoembryonic antigen (CEA) targets were anchored on the MOF through the metal coordination interactions between the hexahistidine (His6) tag in CEA and the unsaturated Cu2+ sites in MOF. The CEA/PQQ-loaded MOF could be captured by the antibody-coated ELISA plate to catalyze the oxidation of cysteine. However, once the target CEA in the samples bound to the antibody immobilized on the plate surface, the attachment of CEA/PQQ-loaded MOF would be limited. Cysteine remaining in the solution would trigger the aggregation of AuNPs and cause a color change from red to blue. The target concentration was positively related to the aggregation and color change of AuNPs. The signal-on competitive plasmonic immunoassay exhibited a low detection limit with a linear range of 0.01–1 ng/mL. Note that most of the proteins in commercial ELISA kits are recombinant with a His6 tag in the N- or C-terminal, so the work could provide a sensitive plasmonic platform for the detection of biomarkers. [ABSTRACT FROM AUTHOR]

The work presented here investigates whether the TpMesFe+ moiety, which had been previously found to mediate the dioxygenation of cysteine and cysteamine, can do the same with simple thiols, which are not functionalized by an amine group. Accordingly, the complexes TpMesFeSR (R=Ph, iPr) were synthesized and after full characterization exposed to O2. They were found to react unselectively to yield sulfinates, disulfides, and thiosulfones as products. The sulfinate complex TpMesFeO2S‐p‐Tol was prepared independently and found to be air‐stable, suggesting that the additional products are not formed via overoxidation or subsequent reactions of coordinated sulfinate product. To investigate whether the larger reaction space, opened up due to the missing amine donor is responsible, a Tp‐ligand functionalized by a pyridyl donor was employed. A corresponding Tp‐iron(II) chlorido complex was prepared and converted through salt metathesis reactions into the respective thiolate analogues, which were fully characterized and structurally authenticated. However, subsequent O2 reactivity studies did not show an improved selectivity. The reason may lie in a more open reaction pocket in combination with an electronic situation which is less ideal than in case of TpMesFe(cysteamine). [ABSTRACT FROM AUTHOR]

Background and Aims: Several studies have highlighted the potent antioxidant properties of N‐acetyl cysteine (NAC). This review aimed to assess the impact of NAC on oxidative stress biomarkers in patients with β‐thalassemia. Methods: The review included articles published before 2024 that investigated the effects of NAC on oxidative stress in individuals with β‐thalassemia. A comprehensive search was conducted across various databases, including Scopus, PubMed, Web of Science, Trip, and CENTRAL. Only English‐language clinical trials were considered for inclusion in this review. Besides, the number needed to treat (NNT) was calculated based on the included studies. Results: Ninety‐nine articles were retrieved from electronic databases, and after a thorough review, eight articles were selected for comprehensive text analysis. The highest dose of NAC administered was 10 mg/kg/day (equivalent to 600 mg/day) over a period of 3–6 months. All the studies assessing the impact of NAC on oxidative stress indicators in β‐thalassemia patients demonstrated positive effects during the 3‐month follow‐up period. Most estimated NNTs fell into 1–5, suggesting significant clinical therapeutic value in this context. Conclusion: The current potency of NAC alone appears to be effective in ameliorating oxidative stress in patients with β‐thalassemia major. While a 3‐month duration seems adequate to demonstrate the antioxidant properties of NAC in this population, larger and well‐designed clinical trials are warranted. Current clinical evidence possesses a high risk of bias. [ABSTRACT FROM AUTHOR]

Posttranslational modifications (PTMs) can modulate the activity, localization and interactions of proteins and (re)define their biological function. Understanding how changing environments can alter cellular processes thus requires detailed knowledge about the dynamics of PTMs in time and space. A PTM that gained increasing attention in the last decades is protein persulfidation, where a cysteine thiol (-SH) is covalently bound to sulfane sulfur to form a persulfide (-SSH). The precise cellular mechanisms underlying the presumed persulfide signaling in plants are, however, only beginning to emerge. In the mitochondrial matrix, strict regulation of persulfidation and H2S homeostasis is of prime importance for maintaining mitochondrial bioenergetic processes because H2S is a highly potent poison for cytochrome c oxidase. This review summarizes the current knowledge about protein persulfidation and corresponding processes in mitochondria of the model plant Arabidopsis. These processes will be compared to the respective processes in non-plant models to underpin similarities or highlight apparent differences. We provide an overview of mitochondrial pathways that contribute to H2S and protein persulfide generation and mechanisms for H2S fixation and de-persulfidation. Based on current proteomic data, we compile a plant mitochondrial persulfidome and discuss how persulfidation may regulate protein function. [ABSTRACT FROM AUTHOR]

Background: This study aims to investigate the causal relationship of human plasma metabolites and metabolic ratios with schizophrenia (SCZ). Methods: We employed Mendelian Randomization (MR) approach to comprehensively analyze two large-scale metabolomics and schizophrenia Genome-Wide Association Study (GWAS) datasets, incorporating a total of 1091 metabolites and 309 metabolic ratios, with 52017 schizophrenia patients and 75889 healthy controls. The inverse variance-weighted (IVW) method was utilized to estimate the causal relationship between exposure and outcome. To provide a more comprehensive evaluation, additional Mendelian Randomization (MR) approaches were employed, including MR-Egger regression, weighted median, simple mode, and weighted mode methods. These analyses assessed the causal effects between blood metabolites, metabolic ratios, and schizophrenia. Tests for pleiotropy and heterogeneity were conducted. False Discovery Rate (FDR) correction was applied to account for multiple comparisons and heterogeneity, ensuring the robustness and reliability of our findings. Consistent with previous studies, an FDR threshold of < 0.2 was considered suggestive of a causal relationship, while an FDR of < 0.05 was considered to indicate a significant causal relationship. Results: The final results revealed that a significant causal association was found between the levels of two metabolites and schizophrenia, Alliin (OR = 0.915, 95%CI = 0.879–0.953, P = 1.93 × 10− 5, FDR = 0.013) was associated with a decreased risk of schizophrenia, N-actylcitrulline (OR = 1.058, 95%CI = 1.034–1.083, P = 1.4 × 10− 6, FDR = 0.002) was associated with increased risk of schizophrenia. When adjusting FDR to 0.2, the results showed that 4 metabolite levels and 2 metabolite ratios were suggestively causally associated with a reduced risk of schizophrenia including 2-aminooctanoate (OR = 0.904, 95%CI = 0.847–0.964, P = 0.002, FDR = 0.160), N-lactoylvaline (OR = 0.853, 95%CI = 0.775–0.938, P = 0.001,FDR = 0.122), X − 21310 (OR = 0.917, 95%CI = 0.866–0.971, P = 0.003,FDR = 0.195), X − 26111 (OR = 0.932, 95%CI = 0.890–0.976, P = 0.003,FDR = 0.189), Arachidonate (20:4n6) to oleate to vaccenate (18:1) ratio (OR = 0.945, 95%CI = 0.914–0.977, P = 8.2 × 10− 4, FDR = 0.104), and Citrulline to ornithine ratio (OR = 0.924, 95%CI = 0.881–0.969, P = 0.001, FDR = 0.122), while 4 metabolite levels and 2 metabolite ratios were suggestively causally associated with an increased risk of schizophrenia including N2, N5-diacetylornithine (OR = 1.090, 95%CI = 1.031–1.153, P = 0.003, FDR = 0.185), N − acetyl − 2−aminooctanoate (OR = 1.069, 95%CI=(1.027–1.114, P = 0.001, FDR = 0.127), N − acetyl − 2−aminoadipate (OR = 1.081, 95%CI = 1.030–1.133, P = 0.001, FDR = 0.128), X − 13844 (OR = 1.110, 95%CI = 1.036–1.190, P = 0.003, FDR = 0.196), X − 24556 (OR = 1.083, 95%CI = 1.036–1.132, P = 4.5 × 10− 4, FDR = 0.098), X − 24736 (OR = 1.065, 95%CI = 1.028–1.104, P = 5.6 × 10− 4, FDR = 0.098), N − acetylasparagine (OR = 1.048, 95%CI = 1.021–1.075, P = 4.5 × 10− 4, FDR = 0.098), N − acetylarginine (OR = 1.060, 95%CI = 1.028–1.092, P = 1.8 × 10− 4, FDR = 0.083), Cysteine to alanine ratio (OR = 1.086, 95%CI = 1.036–1.138, P = 6.5 × 10− 4, FDR = 0.101), and Benzoate to linoleoyl − arachidonoyl − glycerol (18:2 to 20:4) ratio (OR = 1.070, 95%CI = 1.025–1.117, P = 0.002, FDR = 0.158). Conclusion: Our study results provide valuable insights for identifying diagnostic biomarkers related to schizophrenia and offer preliminary research findings for further exploration of the mechanisms linking schizophrenia and metabolism. [ABSTRACT FROM AUTHOR]

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Cys is one of the least abundant amino acids in proteins. However, it is often highly conserved and is usually found in important structural and functional regions of proteins. Its unique chemical properties allow it to undergo several post-translational modifications, many of which are mediated by reactive oxygen, nitrogen, sulfur, or carbonyl species. Thus, in addition to their role in catalysis, protein stability, and metal binding, Cys residues are crucial for the redox regulation of metabolism and signal transduction. In this review, we discuss Cys post-translational modifications (PTMs) and their role in plant metabolism and signal transduction. These modifications include the oxidation of the thiol group (S-sulfenylation, S-sulfinylation and S-sulfonylation), the formation of disulfide bridges, S-glutathionylation, persulfidation, S-cyanylation S-nitrosation, S-carbonylation, S-acylation, prenylation, CoAlation, and the formation of thiohemiacetal. For each of these PTMs, we discuss the origin of the modifier, the mechanisms involved in PTM, and their reversibility. Examples of the involvement of Cys PTMs in the modulation of protein structure, function, stability, and localization are presented to highlight their importance in the regulation of plant metabolic and signaling pathways. [ABSTRACT FROM AUTHOR]

In this study, we investigated the effects of different nitrite sources (sodium nitrite or white kimchi powder) and pink-generating ligands (cysteine, histidine, or nicotinamide) on the development and stability of cured meat color in pork sausage model systems over 30 d of refrigerated storage. The samples were prepared in a 2 × 3 factorial design with two nitrite sources and three ligands, and their physicochemical properties were evaluated on days 0, 15, and 30. Although white kimchi powder induced cured color development similar to that of synthetic sodium nitrite, it resulted in higher cooking loss and lower residual nitrite content in cured pork sausages (p < 0.05). The addition of cysteine resulted in significantly higher CIE a* values, cured meat pigment, and curing efficiency than histidine and nicotinamide (p < 0.05), while yielding lower pH values, residual nitrite content, and total pigment content (p < 0.05). The storage duration significantly reduced the residual nitrite and total pigment contents of the products. These findings suggest that white kimchi powder can serve as a natural alternative to sodium nitrite in pork sausage models and that the incorporation of cysteine has a favorable impact on the development and enhancement of cured meat color. [ABSTRACT FROM AUTHOR]

An imbalance in cysteine (Cys) levels in the cells and plasma has been identified as the risk indicator for various human diseases. The structural similarity of cysteine with its congener homocysteine and glutathione offers challenges in its measurement. Herein, we report a hydrogen‐bonded organic‐inorganic framework of Cu(II) (HOIF) for the selective detection of cysteine over other biothiols. The non‐fluorescent HOIF showed 12‐fold green emission in the presence of cysteine. The monomeric unit of HOIF is stabilized via intermolecular hydrogen bonds, resulting in a non‐porous network structure. Non‐interference from homocysteine, glutathione, and other competitive bio‐analytes revealed explicit affinity of HOIF for cysteine. Fluorimetric titration showed a wide working concentration window (650 nM–800 μM) for measuring cysteine in an aqueous medium. The mechanistic investigation involving HRMS, EPR, and UV‐vis spectroscopic studies revealed the decomplexation of HOIF with Cys, resulting in a fluorescence turn‐on response from the luminescent ligand. Validation using a commercial dye, "Cysteine Green", confirmed the prospect of HOIF for early diagnostic purposes. Utilizing the fluorescence turn‐on property of HOIF in the presence of cysteine, we measured cysteine quantitatively in the blood plasma samples. Bio‐imaging of endogenous cysteine in cancer cells indicated the ability of HOIF to monitor the intracellular cysteine. [ABSTRACT FROM AUTHOR]

This study presents an efficient chemiluminescence (CL) probe based on perovskite nanocrystals (NCs) for detection of L–cysteine (L–Cys). It consists of nickel–doped CsPbBr3 NCs embedded in the mesoporous SiO2 matrix as CL reagent and cerium (IV) as an oxidant in aqueous environment. The probe was designed for the highly selective determination of L–Cys based on its remarkable enhancing effect on the CL intensity. The colloidal nanocomposite of nickel–doped CsPbBr3 NCs@SiO2 with photoluminescence quantum yield of 58% was fabricated by ligand–assisted re–precipitation method and characterized by using UV–Vis absorption, FT–IR, X–ray diffraction, and transmission electron microscopy. The sensor was utilized to determine L–Cys in the linear concentration range of 20–300 nM with a detection limit of 12.8 nM. Direct chemical oxidation of Ni–doped CsPbBr3 NCs@SiO2 by Ce(IV) was the single cause of the formation of the excited-state NCs and subsequent production of CL. The developed probe provides outstanding selectivity towards L–Cys over structurally related compounds. Accurate determination of L–Cys in human serum samples was achieved without interference, and the results were confirmed by HPLC method. [ABSTRACT FROM AUTHOR]

The catalytic hydrogenation of the toxic and harmful p-chloronitrobenzene to produce the value-added p-chloroaniline is an essential reaction for the sustainable chemical industry. Nevertheless, ensuring satisfactory control of its chemoselectivity is a great challenge. In this work, a N/S co-doped metal-free carbon catalyst has been fabricated by using cysteine as a source of C, N, and S. The presence of calcium citrate (porogen agent) in the mixture subjected to pyrolysis provided the carbon with porosity, which permitted us to overcome the issues associated with the loss of heteroatoms during an otherwise necessary activation thermal treatment. Full characterization was carried out and the catalytic performance of the metal-free carbon material was tested in the hydrogenation reaction of p-chloronitrobenzene to selectively produce p-chloroaniline. Full selectivity was obtained but conversion was highly dependent on the introduction of S due to the synergetic effect of S and N heteroatoms. The N/S co-doped carbon (CYSCIT) exhibits a mesoporous architecture which favors mass transfer and a higher doping level, with more exposed N and S doping atoms which act as catalytic sites for the hydrogenation of p-chloronitrobenzene, resulting in enhanced catalytic performance when compared to the N-doped carbon obtained from melamine and calcium citrate (MELCIT) used as a reference. [ABSTRACT FROM AUTHOR]

The neuronal glycine transporter GlyT2 removes glycine from the synaptic cleft through active Na+, Cl−, and glycine cotransport contributing to the termination of the glycinergic signal as well as supplying substrate to the presynaptic terminal for the maintenance of the neurotransmitter content in synaptic vesicles. Patients with mutations in the human GlyT2 gene (SLC6A5), develop hyperekplexia or startle disease (OMIM 149400), characterized by hypertonia and exaggerated startle responses to trivial stimuli that may have lethal consequences in the neonates as a result of apnea episodes. Post‐translational modifications in cysteine residues of GlyT2 are an aspect of structural interest we analyzed. Our study is compatible with a reversible and short‐lived S‐acylation in spinal cord membranes, detectable by biochemical and proteomics methods (acyl‐Rac binding and IP‐ABE) confirmed with positive and negative controls (palmitoylated and non‐palmitoylated proteins). According to a short‐lived modification, direct labeling using click chemistry was faint but mostly consistent. We have analyzed the physiological properties of a GlyT2 mutant lacking the cysteines with high prediction of palmitoylation and the mutant is less prone to be included in lipid rafts, an effect also observed upon treatment with the palmitoylation inhibitor 2‐bromopalmitate. This work demonstrates there are determinants of lipid raft inclusion associated with the GlyT2 mutated cysteines, which are presumably modified by palmitoylation. [ABSTRACT FROM AUTHOR]

BACKGROUND: High moisture meat analog (HMMA) products processed using extrusion have become increasingly popular in the last few years. Because the formation of disulfide bonds is believed to play a critical role in the texturization mechanism, this study aimed to understand how chemical compounds capable of reducing disulfide bonds, specifically cysteine, sodium metabisulfite, and glutathione, affect the texture and the chemical interactions between the proteins. METHOD: Wheat protein blended with cysteine, sodium metabisulfite, or glutathione at levels of 0, 0.5, 1.0, 2.5, 5.0, and 7.5 g kg−1 was extruded at three different temperatures (115, 140, and 165 °C) using a co‐rotating twin‐screw extruder. The feed rate (85 g min−1), the moisture content (600 g kg−1), and the screw speed (300 rpm) were kept constant. Unextruded and extruded material was subjected to sodium dodecyl sulfate‐polyacrylamide gel electrophoresis, polymeric protein fractionation, and sulfhydryl group/disulfide bond analysis. Extruded samples were further analyzed for their hardness and their anisotropic index. RESULTS: The inclusion of reductants significantly affected the structure of the obtained extrudates. Although reducing agents had a relatively small impact on the total amount of disulfide bonds, their action significantly enhanced crosslinking between the proteins. At select conditions, samples with high fibrousness were specifically obtained when cysteine or sodium metabisulfite was included at levels of 5.0 g kg−1. DISCUSSION: In the presence of reducing agents, it is believed that disulfide bonds are split earlier during the process without binding to them, giving the protein strands more time to unravel and align, leading to a better flow behavior and more fibrous products. © 2024 Society of Chemical Industry. [ABSTRACT FROM AUTHOR]

In this work, monodisperse organosilane hybrid polymer microspheres with a particle size of about 5 µm were synthesized using seed swelling polymerization. The organosilicon reagent methacryloxypropyltrimethoxysilane was introduced into the polymer framework as a copolymerization monomer, and the crosslinking degree of the microspheres was improved by the hydrolysis‐condensation reaction of siloxanes. The synthesized hybrid microspheres have good mechanical strength as well as low swelling, with swelling propensity values of 0.167 and 0.348 in methanol and acetonitrile, respectively. Hybrid microspheres modified with cysteine have a hydrophilic interaction chromatography/reversed‐phase liquid chromatography mixed‐mode retention mechanism. Compared to the commercial cysteine‐modified silica column, the synthesized stationary phase has higher separation selectivity for partially acidic or basic samples and better basic resistance for use under high pH mobile phase conditions (at least 10). [ABSTRACT FROM AUTHOR]

This study explored the synthesis and application of BODIPY-functionalized gold nanoparticles (AuNPs) for the sensitive detection of biothiols via an indicator displacement assay coupled with surface-enhanced Raman scattering (SERS) techniques, alongside their efficacy for in vitro cancer cell imaging. Moreover, the assay allowed for the visible colorimetric detection of biothiols under normal and ultraviolet light conditions. The BODIPY (boron-dipyrromethene) fluorophores were strategically conjugated to the surface of gold nanoparticles, forming a robust nanohybrid that leverages the plasmonic properties of AuNPs for enhanced spectroscopic sensitivity. The detection mechanism exploited the displacement of the BODIPY indicator upon interaction with biothiols, triggering a measurable change in fluorescence and SERS signals. This dual-mode sensing approach provides high selectivity and sensitivity for biothiol detection, with detection limits reaching nanomolar concentrations using fluorescence and femtomolar concentration for cysteine using SERS. Furthermore, the BODIPY-AuNP complexes demonstrated excellent biocompatibility and photostability, facilitating their use in the fluorescence imaging of biothiol presence within cellular environments and highlighting their potential for diagnostic and therapeutic applications in biomedical research. [ABSTRACT FROM AUTHOR]

Cysteine redox proteoforms define the diverse molecular states that proteins with cysteine residues can adopt. A protein with one cysteine residue must adopt one of two binary proteoforms: reduced or oxidized. Their numbers scale: a protein with 10 cysteine residues must assume one of 1,024 proteoforms. Although they play pivotal biological roles, the vast cysteine redox proteoform landscape comprising vast numbers of theoretical proteoforms remains largely uncharted. Progress is hampered by a general underappreciation of cysteine redox proteoforms, their intricate complexity, and the formidable challenges that they pose to existing methods. The present review advances cysteine redox proteoform theory, scrutinizes methodological barriers, and elaborates innovative technologies for detecting unique residue-defined cysteine redox proteoforms. For example, chemistry-enabled hybrid approaches combining the strengths of top-down mass spectrometry (TD-MS) and bottom-up mass spectrometry (BU-MS) for systematically cataloguing cysteine redox proteoforms are delineated. These methods provide the technological means to map uncharted redox terrain. To unravel hidden redox regulatory mechanisms, discover new biomarkers, and pinpoint therapeutic targets by mining the theoretical cysteine redox proteoform space, a community-wide initiative termed the "Human Cysteine Redox Proteoform Project" is proposed. Exploring the cysteine redox proteoform landscape could transform current understanding of redox biology. [ABSTRACT FROM AUTHOR]

Peptide therapeutics play an increasingly important role in modern drug discovery. Improving the pharmacokinetic profile of bioactive peptides has been effectively achieved with chemical modifications, especially macrocyclisation reactions. Consequently, there is a great demand for highly constrained compounds such as bicyclic peptides. In our previous research, we introduced peptide–bismuth bicycles and peptide–arsenic bicycles as new classes of constrained peptides. In this work, we extend our peptide bicyclisation strategy towards antimony. Similar to arsenic and bismuth, antimony(III) selectively binds to three cysteine residues in peptides, enabling the in situ formation of stable bicycles. The bicyclisation reaction occurs instantaneously under biocompatible conditions at physiological pH. Antimony–peptide bicycles remain largely intact in the presence of the common metal chelator ethylenediaminetetraacetic acid (EDTA) and the main endogenous thiol competitor glutathione (GSH). Furthermore, when challenged with bismuth(III) from water-soluble gastrodenol (bismuth tripotassium dicitrate), antimony–peptide bicycles convert into the corresponding bismuth–peptide bicycle, highlighting the superior thiophilicity of bismuth over other pnictogens. Our study further expands the toolbox of peptide multicyclisation with main group elements previously underexplored in chemical biology. Cyclic peptide drugs are important therapeutics. Previously, bismuth and arsenic were introduced to create peptide bicycles by binding three cysteines. Now, antimony complements this set of elements to form stable bicyclic peptides. These remain stable in the presence of a common metal chelator and glutathione. Bismuth outcompetes antimony as the core atom in peptide bicycles. (Image credit: Lani Davies.) This article belongs to the 10th Anniversary Collection of RACI and AAS Award papers. [ABSTRACT FROM AUTHOR]

The reactivity of Zn2+ tetrahedral complexes with H2O2 was investigated in silico, as a first step in their disruption process. The substrates were chosen to represent the cores of three different zinc finger protein motifs, i. e., a Zn2+ ion coordinated to four cysteines (CCCC), to three cysteines and one histidine (CCCH), and to two cysteines and two histidines (CCHH). The cysteine and histidine ligands were further simplified to methyl thiolate and imidazole, respectively. H2O2 was chosen as an oxidizing agent due to its biological role as a metabolic product and species involved in signaling processes. The mechanism of oxidation of a coordinated cysteinate to sulfenate‐κS and the trends for the different substrates were rationalized through activation strain analysis and energy decomposition analysis in the framework of scalar relativistic Density Functional Theory (DFT) calculations at ZORA‐M06/TZ2P ae // ZORA‐BLYP‐D3(BJ)/TZ2P. CCCC is oxidized most easily, an outcome explained considering both electrostatic and orbital interactions. The isomerization to sulfenate‐κO was attempted to assess whether this step may affect the ligand dissociation; however, it was found to introduce a kinetic barrier without improving the energetics of the dissociation. Lastly, ligand exchange with free thiolates and selenolates was investigated as a trigger for ligand dissociation, possibly leading to metal ejection; molecular docking simulations also support this hypothesis. [ABSTRACT FROM AUTHOR]

It was previously discovered that, in the Gram-negative bacterium Escherichia coli growing on a minimal medium with sulfate, stress-induced growth arrest is accompanied by the release of hydrogen sulfide. The source of the sulfide is the desulfurization of intracellular cysteine as one of the ways of maintaining it at a safe level. The danger of excess cysteine is associated with its participation in the Fenton reaction, leading to the formation of highly toxic hydroxyl radicals. Using electrochemical sensors, we identified stress-induced sulfide production in the Gram-positive bacteria Bacillus subtilis and Bacillus megaterium, growing on a minimal medium with sulfate, and changes in physiological parameters such as Eh, pH, and oxygen and potassium consumption. Sulfide production was observed during growth arrest due to the depletion of glucose, ammonium or antibiotic action. The use of sensors allowed to continuously record, in growing cultures, even small changes in parameters. There were significant differences in the amount and kinetics of sulfide production between Bacillus and E. coli. These differences are thought to be due to the lack of glutathione in Bacillus. It is suggested that stress-induced sulfide production by Bacillus under the described conditions may be one of the previously unknown sources of hydrogen sulfide in nature. [ABSTRACT FROM AUTHOR]

This document is an editorial introducing a special issue of the journal Biosensors on the topic of advances in optical biosensors and chemical sensors. The editorial provides an overview of the different types of optical sensors, including fluorescence-based sensors, Raman spectroscopy sensing, and fiber optic-based sensors. It summarizes the main contributions in the special issue, highlighting the working mechanisms and applications of each sensor type. The editorial concludes by discussing the current state of the field and future directions for optical sensor technology. [Extracted from the article]

We performed experiments searching for chirality-dependent secondary electron emission for a 141 eV longitudinally spin-polarized electron beam incident on a thick solid cysteine target. We determined the secondary electron yield by measuring the positive current produced when the cysteine target was negatively biased. No spin-dependent effects to a level of 10−3 were found for the secondary electron emission yield. [ABSTRACT FROM AUTHOR]

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Cysteamine (CA) induces duodenal ulcers in rodents (Selye and Szabo, Nature 244:458–459, 1973). Cysteine (Cys), a precursor for the formation of CA (via catabolism of coenzyme A), does not cause lesions in the duodenum (Szabo et al., J Pharmacol Exp Ther 223:68–76, 1982). CA also has antimutagenic and anticancer pharmacology (Fujisawa et al., PLoS ONE 7, 2012; Lee, Adv Pharmacol Pharm Sci 2023:2419444, 2023). We propose a mechanism of CA-induced cell death dependent on oxygen and CA dioxygenase (ADO) that can explain the 50-year-old mystery as to why CA is, but Cys is not, ulcerogenic. Those cells expressing coenzyme A-catabolizing enzymes are subject to a unique type of oxygen- and enzyme-bound-Fe2+-dependent death, type II ferroptosis. [ABSTRACT FROM AUTHOR]

Neurofibromatosis type 1 (NF1) is a prevalent autosomal dominant disorder caused by mutations in the NF1 gene, leading to multisystem disorders. Given the critical role of cysteine residues in protein stability and function, we aimed to identify key NF1 mutations affecting cysteine residues that significantly contribute to neurofibromatosis pathology. To identify the most critical mutations in the NF1 gene that contribute to the pathology of neurofibromatosis, we employed a sophisticated computational pipeline specifically designed to detect significant mutations affecting the NF1 gene. Our approach involved an exhaustive search of databases such as the Human Gene Mutation Database (HGMD), UniProt, and ClinVar for information on missense mutations associated with NF1. Our search yielded a total of 204 unique cysteine missense mutations. We then employed in silico prediction tools, including PredictSNP, iStable, and Align GVGD, to assess the impact of these mutations. Among the mutations, C379R, R1000C, and C1016Y stood out due to their deleterious effects on the biophysical properties of the neurofibromin protein, significantly destabilizing its structure. These mutations were subjected to further phenotyping analysis using SNPeffect 4.0, which predicted disturbances in the protein’s chaperone binding sites and overall structural stability. Furthermore, to directly visualize the impact of these mutations on protein structure, we utilized AlphaFold3 to simulate both the wild-type and mutant NF1 structures, revealing the significant effects of the R1000C mutation on the protein’s conformation. In conclusion, the identification of these mutations can play a pivotal role in advancing the field of precision medicine and aid in the development of effective drugs for associated diseases. [ABSTRACT FROM AUTHOR]

Porphyromonas gingivalis is a keystone pathogen in periodontitis, and Streptococcus sanguinis is an abundant oral commensal bacterium associated with periodontal health. However, the interaction between P. gingivalis and S. sanguinis remains obscure. Here, we established a strategy for high‐throughput measurement of the cell number of P. gingivalis in the coculture with S. sanguinis by detecting the concentration of hydrogen sulfate. The interaction between P. gingivalis and over 2000 S. sanguinis single‐gene mutants was characterized using this strategy, and several interaction‐associated genes in S. sanguinis were determined by detecting more P. gingivalis cells in the coculture with matched S. sanguinis mutants. Three S. sanguinis interaction‐associated genes were predicted to be responsible for cysteine metabolism, and the supplementation of exogenous L‐cysteine promoted the cell number of P. gingivalis in the coculture with S. sanguinis. Thus, exogenous L‐cysteine and the compromised cysteine metabolism in S. sanguinis enhanced the growth of P. gingivalis in the existence of S. sanguinis. Additionally, the interaction between P. gingivalis and other Streptococcus spp. was examined, and S. pneumoniae was the only streptococci that had no inhibition on the cell number of P. gingivalis. In total, this study established a new strategy for high‐throughput screening of the interaction between Streptococcus and P. gingivalis and discovered a set of genes in S. sanguinis that impacted the interaction. The influence of exogenous L‐cysteine on the interaction between P. gingivalis and S. sanguinis in the oral cavity needs further investigation. [ABSTRACT FROM AUTHOR]

Hadal zones account for the deepest 45% of the oceanic depth range and play an important role in ocean biogeochemical cycles. As the least-explored aquatic habitat on earth, hadal ecosystems contain a vast diversity of so far uncultured microorganisms that cannot be grown on conventional laboratory culture media. Therefore, it has been difficult to gain a true understanding of the detailed metabolic characteristics and ecological functions of those difficult-to-culture microorganisms in hadal environments. In this study, a novel anaerobic bacterial strain, MT110T, was isolated from a hadal sediment--water interface sample of the Mariana Trench at 10,890 m. The level of 16S rRNA gene sequence similarity and percentage of conserved proteins between strain MT110T and the closest relatives, Anaerovorax odorimutans DSM 5092T (94.9 and 46.6%) and Aminipila butyrica DSM 103574T (94.4 and 46.7%), indicated that strain MT110T exhibits sufficient molecular differences for genus-level delineation. Phylogenetic analyses based on both 16S rRNA gene and genome sequences showed that strain MT110T formed an independent monophyletic branch within the family Anaerovoracaceae. The combined evidence showed that strain MT110T represents a novel species of a novel genus, proposed as Anoxybacterium hadale gen. nov. sp. nov. (type strain MT110T = KCTC 15922T = MCCC 1K04061T), which represents a previously uncultured lineage of the class Clostridia. Physiologically, no tested organic matter could be used as sole carbon source by strain MT110T. Genomic analysis showed that MT110T had the potential capacity of utilizing various carbon sources, but the pathways of sulfur reduction were largely incomplete. Our experiments further revealed that cysteine is one of the essential nutrients for the survival of strain MT110T, and cannot be replaced by sulfite, leucine, or taurine. This result suggests that organic sulfur compounds might play an important role in metabolism and growth of the family Anaerovoracaceae and could be one of the key factors affecting the cultivation of the uncultured microbes. Our study brings a new perspective to the role of dissolved organic sulfur in hadal ecosystems and also provides valuable information for optimizing the conditions of isolating related microbial taxa from the hadal environment. [ABSTRACT FROM AUTHOR]

Two-pore domain K+ (K2P) channel activity was previously thought to be controlled primarily via a selectivity filter (SF) gate. However, recent crystal structures of TASK-1 and TASK-2 revealed a lower gate at the cytoplasmic pore entrance. Here, we report functional evidence of such a lower gate in the K2P channel K2P17.1 (TALK-2, TASK-4). We identified compounds (drugs and lipids) and mutations that opened the lower gate allowing the fast modification of pore cysteine residues. Surprisingly, stimuli that directly target the SF gate (i.e., pHe., Rb+ permeation, membrane depolarization) also opened the cytoplasmic gate. Reciprocally, opening of the lower gate reduced the electric work to open the SF via voltage driven ion binding. Therefore, it appears that the SF is so rigidly locked into the TALK-2 protein structure that changes in ion occupancy can pry open a distant lower gate and, vice versa, opening of the lower gate concurrently promote SF gate opening. This concept might extent to other K+ channels that contain two gates (e.g., voltage-gated K+ channels) for which such a positive gate coupling has been suggested, but so far not directly demonstrated. Here, the authors identify a cytoplasmic gate in the K2P channel TALK-2 that is strongly positively-coupled to a second gate made up by the selectivity filter. Thereby, stimuli that converge at either gate open both gates, allowing effective polymodal regulation. [ABSTRACT FROM AUTHOR]

Sulfur (S) is an essential element for life on Earth. Plants are able to take up and utilize sulfate (SO42–), the most oxidized inorganic form of S compounds on Earth, through the reductive S assimilatory pathway that couples with photosynthetic energy conversion. Organic S compounds are subsequently synthesized in plants and made accessible to animals, primarily as the amino acid methionine. Thus, plant S metabolism clearly has nutritional importance in the global food chain. S metabolites may be part of redox regulation and drivers of essential metabolic pathways as cofactors and prosthetic groups, such as Fe–S centers, CoA, thiamine, and lipoic acid. The evolution of the S metabolic pathways and enzymes reflects the critical importance of functional innovation and diversifications. Here we review the major evolutionary alterations that took place in S metabolism across different scales and outline research directions that may take advantage of understanding the evolutionary adaptations. [ABSTRACT FROM AUTHOR]

Chemoselective modification of specific residues within a given protein poses a significant challenge, as the microenvironment of amino acid residues in proteins is variable. Developing a universal molecular platform with tunable chemical warheads can provide powerful tools for precisely labeling specific amino acids in proteins. Cysteine and lysine are hot targets for chemoselective modification, but current cysteine/lysine‐selective warheads face challenges due to cross‐reactivity and unstable reaction products. In this study, a versatile fluorescent platform is developed for highly selective modification of cysteine/lysine under biocompatible conditions. Chloro‐ or phenoxy‐substituted NBSe derivatives effectively labeled cysteine residues in the cellular proteome with high specificity. This finding also led to the development of phenoxy‐NBSe phototheragnostic for the diagnosis and activatable photodynamic therapy of GSH‐overexpressed cancer cells. Conversely, alkoxy‐NBSe derivatives are engineered to selectively react with lysine residues in the cellular environment, exhibiting excellent anti‐interfering ability against thiols. Leveraging a proximity‐driven approach, alkoxy‐NBSe probes are successfully designed to demonstrate their utility in bioimaging of lysine deacetylase activity. This study also achieves integrating a small photosensitizer into lysine residues of proteins in a regioselective manner, achieving photoablation of cancer cells activated by overexpressed proteins. [ABSTRACT FROM AUTHOR]

Pseudocontact shifts (PCS) generated by paramagnetic lanthanide ions deliver powerful restraints for protein structure analysis by NMR spectroscopy. We present a new lanthanide tag that generates different PCSs than that of a related tag, which differs in structure by a single oxygen atom. It is highly reactive towards cysteine and performs well in turn-on luminescence and in EPR spectroscopy. [ABSTRACT FROM AUTHOR]

Background and Purpose: The analgesic action of paracetamol involves KV7 channels, and its metabolite N‐acetyl‐p‐benzo quinone imine (NAPQI), a cysteine modifying reagent, was shown to increase currents through such channels in nociceptors. Modification of cysteine residues by N‐ethylmaleimide, H2O2, or nitric oxide has been found to modulate currents through KV7 channels. The study aims to identify whether, and if so which, cysteine residues in neuronal KV7 channels might be responsible for the effects of NAPQI. Experimental Approach: To address this question, we used a combination of perforated patch‐clamp recordings, site‐directed mutagenesis, and mass spectrometry applied to recombinant KV7.1 to KV7.5 channels. Key Results: Currents through the cardiac subtype KV7.1 were reduced by NAPQI. Currents through all other subtypes were increased, either by an isolated shift of the channel voltage dependence to more negative values (KV7.3) or by such a shift combined with increased maximal current levels (KV7.2, KV7.4, KV7.5). A stretch of three cysteine residues in the S2‐S3 linker region of KV7.2 was necessary and sufficient to mediate these effects. Conclusion and Implication: The paracetamol metabolite N‐acetyl‐p‐benzo quinone imine (NAPQI) modifies cysteine residues of KV7 subunits and reinforces channel gating in homomeric and heteromeric KV7.2 to KV7.5, but not in KV7.1 channels. In KV7.2, a triple cysteine motif located within the S2‐S3 linker region mediates this reinforcement that can be expected to reduce the excitability of nociceptors and to mediate antinociceptive actions of paracetamol. [ABSTRACT FROM AUTHOR]

Late-stage specific and selective diversifications of peptides and proteins performed at target residues under ambient conditions are recognized to be the most facile route to various and abundant conjugates. Herein, we report an orthogonal modification of cysteine residues using alkyl thianthreium salts, which proceeds with excellent chemoselectivity and compatibility under mild conditions, introducing a diverse array of functional structures. Crucially, multifaceted bioconjugation is achieved through clickable handles to incorporate structurally diverse functional molecules. This "two steps, one pot" bioconjugation method is successfully applied to label bovine serum albumin. Therefore, our technique is a versatile and powerful tool for late-stage orthogonal bioconjugation. Late-stage specific and selective modifications of peptides and proteins at target residues under ambient conditions are the most facile routes to various bioconjugates. Here, the authors report an orthogonal modification of cysteine residues using alkyl thianthreium salts, which proceeds with excellent chemoselectivity and compatibility under mild conditions, introducing a diverse array of functional structures. [ABSTRACT FROM AUTHOR]

Background: Secreted protein acidic and rich in cysteine (SPARC) has been shown to modulate aggressive behavior in several benign and malignant tumors. Little is known about SPARC expression in odontogenic keratocyst (OKC), an odontogenic cyst with an aggressive nature. To the best of our knowledge, only one study has been investigated the expression of this protein in OKCs. This study aimed to characterize SPARC expression in OKCs. Additionally, to determine whether SPARC is associated with aggressive behavior in OKCs, SPARC expression in OKCs was compared with radicular cysts (RCs), dentigerous cysts (DCs) and calcifying odontogenic cysts (COCs). These odontogenic cysts showed no or less aggressive behavior. Methods: SPARC expression was evaluated in 38 OKCs, 39 RCs, 35 DCs and 14 COCs using immunohistochemistry. The percentages of positive cells and the intensities of immunostaining in the epithelial lining and the cystic wall were evaluated and scored. Results: Generally, OKCs showed similar staining patterns to RCs, DCs and COCs. In the epithelial lining, SPARC was not detected, except for ghost cells in all COCs. In the cystic wall, the majority of positive cells were fibroblasts. Compared between 4 groups of odontogenic cysts, SPARC expression in OKCs was significantly higher than those of RCs (P < 0.001), DCs (P < 0.001) and COCs (P = 0.001). Conclusions: A significant increase of SPARC expression in OKCs compared with RCs, DCs and COCs suggests that SPARC may play a role in the aggressive behavior of OKCs. [ABSTRACT FROM AUTHOR]

Background: The prevalence of sarcopenia is increasing in worldwide with accelerated aging process. The high dietary protein intakes are associated with improved muscle mass and strength especially in Asian countries. However, there are few researches on amino acid levels or mechanism exploration. We conducted a case-control study to explore the amino acid metabolic characteristics and potential mechanism of elderly women with sarcopenia using targeted amino acid metabolomics approach combined with an analysis of dietary intake. Methods: For our case-control study, we recruited women (65–75 y) from a Shanghai community with 50 patients with sarcopenia and 50 healthy controls. The consensus updated by the Asian Working Group on Sarcopenia in 2019 was used to screening for sarcopenia and control groups. We collected fasting blood samples and evaluated dietary intake. We used the amino acid-targeted metabolomics by ultra performance liquid chromatography tandem mass spectrometry to identify metabolic differentials between the case and control groups and significantly enriched metabolic pathways. Results: The case (sarcopenia) group had a lower intake of energy, protein, and high-quality protein (P < 0.05) compared to the control (healthy) group. We identified four differential amino acids: arginine (P < 0.001) and cystine (P = 0.003) were lower, and taurine (P = 0.001) were higher in the case group. Conclusion: Low levels of arginine in elderly women are associated with a higher risk of sarcopenia. [ABSTRACT FROM AUTHOR]

The toxicity of silver nanoparticles (AgNPs) depends on their physicochemical properties. The ongoing research aims to develop effective methods for modifying AgNPs using molecules that enable control over the processes induced by nanoparticles in both normal and cancerous cells. Application of amino acid-stabilized nanoparticles appears promising, exhibiting tunable electrokinetic properties. Therefore, this study focused on determining the influence of the surface charge of cysteine (CYS)-stabilized AgNPs on their toxicity towards human normal B (COLO-720L) and T (HUT-78) lymphocyte cell lines. CYS-AgNPs were synthesized via the chemical reduction. Transmission electron microcopy (TEM) imaging revealed that they exhibited a quasi-spherical shape with an average size of 18 ± 3 nm. CYS-AgNPs remained stable under mild acidic (pH 4.0) and alkaline (7.4 and 9.0) conditions, with an isoelectric point observed at pH 5.1. Following a 24 h treatment of lymphocytes with CYS-AgNPs, concentration-dependent alterations in cell morphology were observed. Positively charged CYS-AgNPs notably decreased lymphocyte viability. Furthermore, they exhibited grater genotoxicity and more pronounced disruption of biological membranes compared to negatively charged CYZ-AgNPs. Despite both types of AgNPs interacting similarly with fetal bovine serum (FBS) and showing comparable profiles of silver ion release, the biological assays consistently revealed that the positively charged CYS-AgNPs exerted stronger effects at all investigated cellular levels. Although both types of CYS-AgNPs have the same chemical structure in their stabilizing layers, the pH-induced alterations in their surface charge significantly affect their biological activity. [ABSTRACT FROM AUTHOR]

Modern society's keen regard for aesthetics made hair products an integral part of a multi‐billion‐dollar cosmetic industry. Hair care products (e.g., shampoos and conditioners) and chemical treatments (e.g., bleaching and permanent waving) result in various effects on the morphological attributes of hair. Generally, water adsorbed on the hair surface is known to significantly dictate the hair's mechanical characteristics (smoothness and friction), and hair's macroscopic wettability has been commonly used to indicate its surface properties. However, an approach to selectively characterize the hydration water in the hair surface is required to accurately understand the intermolecular events between the hair and its vicinal water. In this paper, we successfully obtained the infrared (IR) absorption spectra of the hydration water of human hair. We employed the multivariate curve resolution‐alternating least square (MCR‐ALS) method to separate the hydration and bulk water spectra from the whole spectra. Comparing the IR spectra of the hydration water of chemically untreated and bleached hair samples, we conclude that water molecules form strong hydrogen bonds with the bleached hair surface due to the destruction of the hair's hydrophobic outer layer and the consequent formation of hydrophilic residues. [ABSTRACT FROM AUTHOR]

Much progress has been made in the determination of As (III), while numerous electrochemical sensors based on metal nanomaterials with significant sensitivity and precision have been developed. However, further research is still required to achieve rapid detection and avoid interference from other metal ions (especially copper ions). In this study, bimetallic AuPt nanoparticles are electrochemically modified with screen printing electrodes. What's more, L-cysteine also self-assembles with AuNPs through Au-S bond to enhance the electrochemical performance. To overcome the interference of Cu (II) in the sensing process, the reduced iron powder was chosen to remove Cu (II) and other oxidizing organics in aqueous solutions. The lowest detectable amount is 0.139 ppb, a linear range of 1~50 ppb with superlative stability by differential pulse anodic stripping voltammetry. Fortunately, the reduced iron powder could eliminate the Cu (II) with no effect on the As (III) signal. [ABSTRACT FROM AUTHOR]

A novel accelerator, cerium cysteine (Ce-Cys) was synthesised by double replacement reaction. The complex was characterised by FT-IR analysis, thermal analysis, EDTA titration and elemental analysis, respectively, to determine that the molecular formula of the complex was Ce (Cys)3Cl3·3H2O. Cure characteristics, crosslink density, mechanical properties and thermo-oxidative ageing of NR compounds were investigated. The research revealed that the vulcanisates containing Ce-Cys manifested high scorch time, outstanding mechanical properties, and better thermo-oxidative ageing properties. Furthermore, based on kinetic calculations, it was concluded that as the amount of Ce-Cys increased, the reactivity of the crosslink precursor increased while the activation energy decreased. [ABSTRACT FROM AUTHOR]

Cysteine thiols are susceptible to various oxidative posttranslational modifications (PTMs) due to their high chemical reactivity. Thiol‐based PTMs play a crucial role in regulating protein functions and are key contributors to cellular redox signaling. Although reversible thiol‐based PTMs, such as disulfide bond formation, S‐nitrosylation, and S‐glutathionylation, have been extensively studied for their roles in redox regulation, thiol sulfinic acid (–SO2H) modification is often perceived as irreversible and of marginal significance in redox signaling. Here, we revisit this narrow perspective and shed light on the redox regulatory roles of –SO2H in plant stress signaling. We provide an overview of protein sulfinylation in plants, delving into the roles of hydrogen peroxide‐mediated and plant cysteine oxidase‐catalyzed formation of –SO2H, highlighting the involvement of –SO2H in specific regulatory signaling pathways. Additionally, we compile the existing knowledge of the –SO2H reducing enzyme, sulfiredoxin, offering insights into its molecular mechanisms and biological relevance. We further summarize current proteomic techniques for detecting –SO2H and furnish a list of experimentally validated cysteine –SO2H sites across various species, discussing their functional consequences. This review aims to spark new insights and discussions that lead to further investigations into the functional significance of protein –SO2H‐based redox signaling in plants. Summary statement: This review expands upon the conventional understanding of cysteine thiol sulfinic acid modification and provides an updated overview of its redox‐dependent regulatory functions in the context of plant stress signaling pathways. [ABSTRACT FROM AUTHOR]

Native liquid chromatography mass spectrometry (LC-MS) is a commonly used approach for intact analysis of inter-chain cysteine conjugated antibody-drug conjugates (ADCs). Coupling native LC-MS with affinity capture provides a platform for intact ADC analysis from in vivo samples and characterisation of individual drug load species, specifically the impact of drug linker deconjugation, hydrolysis, and differential clearance in a biological system. This manuscript describes data generated from native LC-MS analysis of ADCs from human plasma, both in vitro incubations and clinical samples. It also details the pharmacokinetic (PK) model built to specifically characterise the disposition of individual drug load species from MMAE and MMAF interchain cysteine conjugated ADCs. In vitro deconjugation and hydrolysis rates were similar across both ADCs. Differential clearance of higher loaded species in vivo was pronounced for the MMAE conjugated ADC, while systemic elimination after accounting for deconjugation was similar across drug loads for the MMAF conjugated ADC. This is the first report of affinity capture native LC-MS analysis, and subsequent modelling of deconjugation, hydrolysis and clearance rates of individual drug load species using clinical data from cysteine conjugated ADCs. [ABSTRACT FROM AUTHOR]