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Protein–calixarenes binding plays an increasingly central role in many applications, spanning from molecular recognition to drug delivery strategies and protein inhibition. These ligands obey a specific bio-supramolecular chemistry, which can be revealed by computational approaches, such as molecular dynamics simulations. In this paper, we rely on all-atom, explicit-solvent molecular dynamics simulations to capture the electrostatically driven association of a phosphonated calix-[4]-arene with cytochome-C, which critically relies on surface-exposed paired lysines. Beyond two binding sites identified in direct agreement with the x-ray structure, the association has a larger structural impact on the protein dynamics. Then, our simulations allow a direct comparison to analogous calixarenes, namely, sulfonato, similarly reported as "molecular glue." Our work can contribute to a robust in silico predictive tool to assess binding sites for any given protein of interest for crystallization, with the specificity of a macromolecular cage whose endo/exo orientation plays a role in the binding. [ABSTRACT FROM AUTHOR]

In this paper, we present Raman imaging as a non-invasive approach for studying changes in mitochondrial metabolism caused by cardiolipin–cytochrome c interactions. We investigated the effect of mitochondrial dysregulation on cardiolipin (CL) and cytochrome c (Cyt c) interactions for a brain cancer cell line (U-87 MG). Mitochondrial metabolism was monitored by checking the intensities of the Raman bands at 750 cm−1, 1126 cm−1, 1310 cm−1, 1337 cm−1, 1444 cm−1 and 1584 cm−1. The presented results indicate that under pathological conditions, the content and redox status of Cyt c in mitochondria can be used as a Raman marker to characterize changes in cellular metabolism. This work provides evidence that cardiolipin–cytochrome c interactions are crucial for mitochondrial energy homeostasis by controlling the redox status of Cyt c in the electron transport chain, switching from disabling Cyt c reduction and enabling peroxidase activity. This paper provides experimental support for the hypothesis of how cardiolipin–cytochrome c interactions regulate electron transfer in the respiratory chain, apoptosis and mROS production in mitochondria. [ABSTRACT FROM AUTHOR]

Kaempferol (KAE) is a natural flavonoid with powerful reactive oxygen species (ROS) scavenging properties and beneficial effects on ex vivo sperm functionality. In this paper, we studied the ability of KAE to prevent or ameliorate structural, functional or oxidative damage to frozen–thawed bovine spermatozoa. The analysis focused on conventional sperm quality characteristics prior to or following thermoresistance tests, namely the oxidative profile of semen alongside sperm capacitation patterns, and the levels of key proteins involved in capacitation signaling. Semen samples obtained from 30 stud bulls were frozen in the presence of 12.5, 25 or 50 μM KAE and compared to native ejaculates (negative control—CtrlN) as well as semen samples cryopreserved in the absence of KAE (positive control—CtrlC). A significant post-thermoresistance test maintenance of the sperm motility (p < 0.001), membrane (p < 0.001) and acrosome integrity (p < 0.001), mitochondrial activity (p < 0.001) and DNA integrity (p < 0.001) was observed following supplementation with all KAE doses in comparison to CtrlC. Experimental groups supplemented with all KAE doses presented a significantly lower proportion of prematurely capacitated spermatozoa (p < 0.001) when compared with CtrlC. A significant decrease in the levels of the superoxide radical was recorded following administration of 12.5 (p < 0.05) and 25 μM KAE (p < 0.01). At the same time, supplementation with 25 μM KAE in the cryopreservation medium led to a significant stabilization of the activity of Mg2+-ATPase (p < 0.05) and Na+/K+-ATPase (p < 0.0001) in comparison to CtrlC. Western blot analysis revealed that supplementation with 25 μM KAE in the cryopreservation medium prevented the loss of the protein kinase A (PKA) and protein kinase C (PKC), which are intricately involved in the process of sperm activation. In conclusion, we may speculate that KAE is particularly efficient in the protection of sperm metabolism during the cryopreservation process through its ability to promote energy synthesis while quenching excessive ROS and to protect enzymes involved in the process of sperm capacitation and hyperactivation. These properties may provide supplementary protection to spermatozoa undergoing the freeze–thaw process. [ABSTRACT FROM AUTHOR]

As compounds of natural origin enter human body, it is necessary to investigate their possible interactions with the metabolism of drugs and xenobiotics in general, namely with the cytochrome P450 (CYP) system. Phytic acid (myo-inositol hexaphosphoric acid, IP6) is mainly present in plants but is also an endogenous compound present in mammalian cells and tissues. It has been shown to exhibit protective effect in many pathological conditions. For this paper, its interaction with CYPs was studied using human liver microsomes, primary human hepatocytes, the HepG2 cell line, and molecular docking. Docking experiments and absorption spectra demonstrated the weak ability of IP6 to interact in the heme active site of CYP1A. Molecular docking suggested that IP6 preferentially binds to the protein surface, whereas binding to the active site of CYP1A2 was found to be less probable. Subsequently, we investigated the ability of IP6 to modulate the metabolism of xenobiotics for both the mRNA expression and enzymatic activity of CYP1A enzymes. Our findings revealed that IP6 can slightly modulate the mRNA levels and enzyme activity of CYP1A. However, thanks to the relatively weak interactions of IP6 with CYPs, the chances of the mechanisms of clinically important drug–drug interactions involving IP6 are low. [ABSTRACT FROM AUTHOR]

In this paper, a new genus in the nudibranch family Discodorididae, Avaldesia n. gen. is established for Avaldesia albomacula (Chan & Gosliner, 2007) and Avaldesia tahala (Chan & Gosliner, 2007), originally assigned to the genus Thordisa Bergh, 1877, and a new species, Avaldesia tamatoa n. sp. described here from the central Pacific. To establish species relationships within Avaldesia , as well as the placement of Avaldesia within Discodorididae, we utilized four molecular markers (cytochrome c oxidase subunit I, 16S rRNA, histone H3 and 28S rRNA) in our Bayesian inference and maximum likelihood analyses. Four species delimitation methods were complemented by morphological dissections and scanning electron microscopy. Our results reveal a clear separation between Avaldesia and Thordisa and suggest that Avaldesia is more closely related to the genera Hoplodoris Bergh, 1880 and Asteronotus Ehrenberg, 1831. The most characteristic features of Avaldesia include a radula with increasing denticulation towards the fimbriate outermost laterals and a reproductive system with a lobate vestibular gland, occasional hollow vestibular spine and a penis armed with one or more penial spines. All species of Avaldesia are found in shallow water (5–10 m depth) on rocky reefs, sandy sediments and algal fields with distributions across the Indo-Pacific. [ABSTRACT FROM AUTHOR]

The Journal of Alzheimer's Disease has retracted an article titled "Cyclosporin A inhibits Al-induced cytochrome c release from mitochondria in aged rabbits" due to ethical concerns regarding Figure 1. The first author and senior/last author of the paper are retired and no longer have access to the original data. Additionally, the validity of some representative images has been called into question. As a result, the Editorial Office has decided to retract the paper. [Extracted from the article]

The concentration of cytochrome C is demonstrated to be an effective indicator of the microbial corrosion strength of metals. Traditional cytochrome C sensor can detect cytochrome C with a low detection limit, but their use is limited by their high cost, cumbersome operation, and susceptibility to malignant environments. In addition, studies on the monitoring of cytochrome C in the field of microbial corrosion has still not been carried out. Therefore, there is a need for a highly sensitive, selective, low-cost, anti-interference, and stable cytochrome C sensor with online monitoring and remote sensing capabilities for in-situ measurement of microbial corrosion strength. This paper proposed a highly sensitive label-free fiber-optic sensor based on Mach-Zehnder interferometer (MZI) for in-situ measurement of the microbial corrosion marker cytochrome C. Two-dimensional Ti 2 C-MXene material is uniformly immobilized onto the surface of the sensing area to improve the sensitivity, hydrophilicity, and specific surface area of the sensing area, as well as to facilitate the immobilization of specific sensitive materials. The cytochrome C antibody is modified on the surface of Ti 2 C-MXene to specifically recognize cytochrome C, whose concentration variation can be measured by monitoring the spectral shift of MZI sensor. Results demonstrate a measurement sensitivity of 1.428 nm/μM for cytochrome C concentrations ranging from 0 to 7.04 μM. The detection limit of the sensor is calculated to be 0.392 μM with remarkable performance, including selectivity, stability, and reliability. Besides, the measurement result of the proposed sensor in real microbial corrosive environment is consistent with that of the ideal environment. This is the first instance of achieving in-situ and label-free measurement of cytochrome C by using a fiber-optic MZI sensor, which undoubtedly provides a feasible solution for the effective monitoring of microbial metal corrosion in the environment. [Display omitted] • A transverse mismatched MZI with a strong evanescent field is proposed. • Ti 2 C-MXene is used as a sensitizing material to increase the penetration depth of evanescent wave. • In situ and label-free measurements of cytochrome C were achieved. • The strength of microbial corrosion in complex environments can be monitored in real-time. [ABSTRACT FROM AUTHOR]