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The present paper deals with the physiological response of the changes in chemical contents in the root, stem and leaf of Vetiveria zizanioides seedlings stressed by excess cadmium using Fourier transform infrared spectroscopy technique. Cadmium accumulation in plant and distribution in subcellular by atomic absorption spectroscopy were tested under different concentrations cadmium stress. The results show that low cadmium concentrations (

Photocatalytic hydrogen (H2) evolution integrated with selective oxidation to produce fine chemicals is a promising strategy for solar energy conversion and storage; however, the efficiency of such coupled photocatalytic redox cycles is greatly limited by the poor surface kinetics of hydrogen evolution reaction (HER) and/or dehydrogenation reaction (DHR) on heterogenous photocatalysts. Herein, we demonstrate that the immobilization of ultrafine nickel disulfide (NiS2) nanoparticles on CdS nanosheets (NiS2/CdS) is a simple yet efficient approach to kinetic improve the surface redox reactions for H2 production and dehydrogenative coupling of amines to imines. The NiS2 nanoparticles loaded on CdS not only function as the HER active sites to speed up charge separation and to boost H2 release, but also enhance the adsorption of amines to facilitate the dissociation of C-H and N-H bonds to form aldimines intermediates, which are readily coupled with other amines to afford a high selectivity toward imine synthesis. Benefiting from such unique bifunctional catalytic behavior of NiS2 in proton (H+) reduction and substrate activation, NiS2/CdS exhibits a remarkable enhanced photocatalytic performance toward simultaneous production of H2 and imines. The apparent quantum efficiency (AQE) at 420 nm is calculated to be 54.7%. This strategy using bifunctional cocatalysts to kinetic improve the surface redox reactions will have broad implications in the development of high-performance photocatalysts for integrated production of solar hydrogen and value-added solar chemicals.

Photocatalytic benzene hydroxylation reaction using a clean oxidant such as H2O2 is a green synthetic approach for phenol synthesis. Here, our study shows that silylated iron vanadate (FeVO4) nanorods can function as promising photocatalysts to direct hydroxylation of benzene to phenol, by taking advantage of the unique benefits of covalently bonded organosilane (OS) groups to realize kinetic control of heterogeneous photocatalytic reactions. The grafting of OS functional groups on FeVO4 helps to tailor its surface affinity to fine-tune the benzene adsorption behavior and photo-Fenton process for H2O2 activation. In addition, the OS groups immobilized on the FeVO4 surface via a rather strong Si–O bond also serve as an effective protective coating to suppress metal leaching, thus affording FeVO4 with an excellent stability to undergo a heterogeneous photo-Fenton process. As a result, the silylated FeVO4 exhibits robust photocatalytic benzene hydroxylation performance. The phenol yield and selectivity obtained on the optimized silylated FeVO4 are determined to be 20% and 98%, much better than that obtained from pristine FeVO4. Benefiting from its robust stability and tunable surface affinity, the silylated FeVO4 will have broad applications in photocatalytic selective oxidation to produce fine chemicals.

With the accelerated urbanization and rapid development of the industrial and agricultural sectors, concern about the pollution of water environments is becoming more widespread. Algal blooms of varying sizes are becoming increasingly frequent in lakes and reservoirs; temperatures, nutrients, heavy metals, and dissolved oxygen are the factors that influence algal bloom occurrence. However, knowledge of the combined effect of heavy metals and temperature on algal growth remains limited. Thus, this study investigated how specific concentrations of heavy metals affect algal growth at different temperatures; to this end, two heavy metals were used (0.01 mg/L Pb2+ and 0.05 mg/L Cr6+) at three incubation temperatures (15, 25, and 30 °C) with the alga Chlorella sp. A higher incubation temperature contributed to a rise in soluble proteins, which promoted algal growth. The density of algal cells increased with temperature, and catalase (CAT) decreased with increasing temperature. Chlorella sp. growth and catalase activity were optimal at 30 °C (algal cell density: 1.46 × 107 cell/L; CAT activity: 29.98 gprot/L). Pb2+ and Cr6+ significantly promoted Chlorella sp. growth during incubation at 25 and 30 °C, respectively. At specific temperatures, 0.01 mg/L Pb2+ and 0.05 mg/L Cr6+ promoted the production of soluble proteins and, hence, the growth of Chlorella sp. The results provide a useful background for the mitigation and prevention of algal blooms.

The aggregation of human islet amyloid polypeptide (hIAPP) is one of the triggering factors of type 2 diabetes mellitus (T2DM). hIAPP is cosynthesized, costored, and cosecreted with insulin in pancreatic β-cells, and insulin inhibits hIAPP aggregation. In T2DM patients, long-term hyperglycemia causes glycation of near 10% of total insulin. The glycation not only modifies insulin but also cross-links insulin into oligomers. However, the effect of glycated human insulin on hIAPP aggregation is unknown. In this study, four physiologically relevant monosaccharides, methylglyoxal, glucose, fructose, and ribose were used to glycate human insulin and two C-terminus truncated insulin analogues. Glycated insulin monomers or low molecular weight oligomers such as dimers significantly exacerbated the cytotoxicity of hIAPP. Notably, glycation-induced cross-linking of insulin inhibited the aggregation, membrane disruption, and cytotoxicity of hIAPP, which was corroborated by a control study using EGS-induced cross-linking of insulin or lysozyme. Removal of B29

Background The misfolding of human islet amyloid polypeptide (hIAPP) is an important pathological factor on the onset of type 2 diabetes. A number of studies have been focused on His 18 , the only histidine of hIAPP, whose imidazole ring and the protonation state might impact hIAPP amyloid formation, but the exact mechanism remains unclear. Methods We used diethylpyrocarbonate (DEPC) to specifically modify His 18 and obtained mono-ethyloxyformylated hIAPP (DMI). Thioflavin T based fluorescence, transmission electronic microscopy, circular dichroism spectroscopy, fluorescence dye leakage, Fourier transform infrared spectroscopy and replica-exchange molecular dynamics (REMD) simulation were applied to study the impact of DEPC-modification on hIAPP amyloid formation. Results After an ethyl-acetate group was introduced to the His 18 of hIAPP by diethylpyrocarbonate (DEPC) modification, the pH dependent hIAPP fibrillation went to the opposite order and the number of intra-molecular hydrogen bonds decreased, while the possibility of His 18 participating in the formation of α-helical structures increased. Furthermore, the membrane–peptide interaction and ion–peptide interaction were both impaired. Conclusions The intramolecular hydrogen bond formation by His 18 and the possibility of His 18 participating in the formation of α-helical structures greatly modulated the manner of hIAPP amyloid formation. The imidazole ring directly participates in the hIAPP–membrane/ion interaction. General significance DEPC modification is an alternative approach to investigate the role of the imidazole ring during amyloid formation.

Hypofibrinolysis is commonly found in patients with diabetes mellitus and is associated with the increased risk for many diabetic complications. An important inhibitor of fibrinolysis, thrombin-activatable fibrinolysis inhibitor (TAFI), participates in hypofibrinolysis in diabetes mellitus and may be involved in diabetic macrovascular disease. The present study was designed to determine whether TAFI polymorphisms (505G/A and 1040C/T) and TAFI levels are correlated with the development of type 2 diabetes mellitus (T2DM) and macrovascular diseases (MVDs). A total of 249 clinical samples were collected, including 102 healthy individuals (H group), 44 T2DM patients without MVD (T group) and 103 T2DM patients with MVD (M group). The 505G/A polymorphism was equally represented in the three groups. In contrast, analysis of the 1040C/T polymorphism revealed a statistically lower percentage of the T allele in the M group than in the H group (P = 0.014). This difference was due to decreased T/T homozygotes in the M groups compared with the H group (P = 0.029). The antigen TAFI level was 31.72 ± 13.64% in the H group, 62.56 ± 18.77% in the T group (P

Cinnamon consumption has been found to associate with the attenuation of diabetes mellitus. The misfolding of human islet amyloid polypeptide (hIAPP) is regarded as a causative factor of type 2 diabetes mellitus (T2DM). Here, we investigated whether cinnamon has any beneficial effect on the toxic aggregation of hIAPP. We found that cinnamon water extract (CWE) inhibited the amyloid formation of hIAPP in a dose-dependent manner, and identified proanthocyanidins as the major anti-amyloidogenic compounds of CWE. Proanthocyanidins affected the secondary structures of hIAPP and delayed the structural transition from unstructured coils to β-sheet-rich structures. Further studies showed that proanthocyanidins not only inhibited the formation of hIAPP oligomers, but also significantly attenuated the membrane damaging and cytotoxic effects caused by the hIAPP aggregation. Together, these results suggest a possible way by which cinnamon shows beneficial effects on T2DM, and indicate a potential pharmacological usage of proanthocyanidins as an anti-diabetic drug candidate.

Long-term hyperglycemia is a typical symptom of diabetes mellitus (DM) which can cause a high level of protein glycation and lead to the formation of advanced glycation end products (AGEs). The accumulation of AGEs in turn deteriorates DM and its complications. Insulin, the only hormone that directly decreases blood sugar in vivo, is vulnerable to glycation which causes the loss of its biological activity. In this study, we used a porcine insulin (PI)–methylglyoxal (MGO) model to investigate the inhibitory effect of leonurine (LN), a natural alkaloid extracted from Herba leonuri, on AGE formation. Assays including AGE-specific fluorescence, and fructosamine level and carbonyl group content determination showed that LN can dose-dependently suppress PI glycation. A significantly decreased cross-linking level on the glycated PI was also proven by SDS-PAGE electrophoresis. A further liquid chromatography-mass spectrometry study suggested that LN may inhibit PI glycation through trapping MGO and keeping it from reacting with PI. Our results thus indicate that LN is a promising anti-glycation agent for the prevention of diabetes and its complications via inhibiting AGE formation.

The process of protein aggregation from soluble amyloidogenic proteins to insoluble amyloid fibrils plays significant roles in the onset of over 30 human amyloidogenic diseases, such as Prion disease, Alzheimer's disease and type 2 diabetes mellitus. Amyloid deposits are commonly found in patients suffered from amyloidosis; however, such deposits are rarely seen in healthy individuals, which may be largely attributed to the self-regulation in vivo. A vast number of physiological factors have been demonstrated to directly affect the process of amyloid formation in vivo. In this review, physiological factors that influence amyloidosis, including biological factors (chaperones, natural antibodies, enzymes, lipids and saccharides) and physicochemical factors (metal ions, pH environment, crowding and pressure, etc.), together with the mechanisms underlying these proteostasis effects, are summarized.

More than 30 amyloid proteins are reported to be associated with amyloidosis diseases. Studies have implicated histidine may be critically involved in amyloid formation. Here, we used diethylpyrocarbonate (DEPC) modification to obtain a His(B5) mono-ethyloxyformylated insulin (DMI-B(5)). The secondary structure, amyloidogenicity, metal ion interaction, and cytotoxicity of DMI-B(5) and insulin were compared. DMI-B(5) was less prone to aggregation in acidic condition but easier to aggregate at neutral pH. DEPC modification resulted in attenuated inhibitory effect of Zn(2+) on aggregation, whereas DMI-B(5) fibrils induced more severe erythrocytes haemolysis compared to insulin fibrils. This study not only provides a fast new approach for studying the impact of imidazole ring in amyloid formation, but also reveals the critical modulating role of histidine imidazole ring on the amyloidogenicity of insulin.

It is widely accepted that the formation of amyloid fibrils is one of the natural properties of proteins. The amyloid formation process is associated with a variety of factors, among which the hydrophobic residues play a critical role. In this study, insulin was used as a model to investigate the effect of exposing a critical hydrophobic patch on amyloidogenicity and fibril structure of insulin. Porcine insulin was digested with trypsin to obtain desoctapeptide-(B23–B30) insulin (DOI), whose hydrophilic C-terminal of B-chain was removed and hydrophobic core was exposed. The results showed that DOI, of which the ordered structure (predominantly α-helix) was markedly decreased, was more prone to aggregate than intact insulin. As to the secondary structure of amyloid fibrils, DOI fibrils were similar to insulin fibrils formed under acidic condition, whereas under neutral condition, insulin formed less polymerized aggregates by showing decreased β-sheet contents in fibrils. Further investigation on membrane damage and hemolysis showed that DOI fibrils induced significantly less membrane damage and less hemolysis of erythrocytes compared with those of insulin fibrils. In conclusion, exposing the hydrophobic core of insulin can induce the increase of amyloidogenicity and formation of higher-order polymerized fibrils, which is less toxic to membranes.

Global epidemic studies have suggested that coffee consumption is reversely correlated with the incidence of type 2 diabetes mellitus (T2DM), a metabolic disease. The misfolding of human islet amyloid polypeptide (hIAPP) is regarded as one of the causative factors of T2DM. Coffee extracts have three major active components: caffeine, caffeic acid (CA), and chlorogenic acid (CGA). In this study, the effects of these major coffee components, as well as dihydrocaffeic acid (DHCA) (a major metabolite of CGA and CA), on the amyloidogenicity of hIAPP were investigated by thioflavin-T based fluorescence emission, transmission electronic microscopy, circular dichroism, light-induced cross-linking, dynamic light scattering, and MTT-based cell viability assays. The results suggest that all components show varied inhibitory effects on the formation of toxic hIAPP amyloids, in which CA shows the highest potency in delaying the conformational transition of the hIAPP molecule with the most prolonged lag time, whereas caffeine shows the lowest potency. At a 5-fold excess molar ratio of compound to hIAPP, all coffee-derived compounds affect the secondary structures of incubated hIAPP as suggested by the circular dichroism spectra and CDPro deconvolution analysis. Further photoinduced cross-linking based oligomerization and dynamic light scattering studies suggested CA and CGA significantly suppressed the formation of hIAPP oligomers, whereas caffeine showed no significant effect on oligomerization. Cell protection effects were also observed for all three compounds, with the protection efficiency being greatest for CA and least for CGA. These findings suggest that the beneficial effects of coffee consumption on T2DM may be partly due to the ability of the major coffee components and metabolites to inhibit the toxic aggregation of hIAPP.