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Volokh, O.

Publications and source records attributed to Volokh, O..

2 recordsLinked to original sources

Peptidome and Metabolome profiling of the fermented milk products revealed accumulation of bioactive compounds during two weeks of cold storage

This study assessed the metabolome and peptidome profiles of various fermented milk products produced using different starter cultures. Milk fermentation involves a set of macromolecular decomposition reactions performed by microorganisms under controlled conditions. Biotransformation of fats, proteins, and carbohydrates shapes the metabolome profile of each fermented product. Many of these microbe-generated molecules exhibit biological activities that can affect human health. The resulting profile is unique for every fermented product and depends on technology, raw materials, and starter culture composition. We used four non-targeted metabolomic methods to assess semi-quantified concentrations of four types of molecules in the final products: peptides; amino acids; long-, medium-, and short-chain fatty acids; mono- and disaccharides and their derivatives. Ultra-performance liquid chromatography-mass spectrometry (UPLC-MS/MS) was performed on the peptidome. For all other fractions, we used gas chromatography-mass spectrometry (GC-MS), with a method adapted to specific metabolite conditions. Metabolome and peptidome of four groups of 15 dairy cow milk products including yogurt (Y), fermented milk (FM), kefir made with commercial cultures (K) and kefir made with grains (KG) was performed on days 7 and 14 of shelf life at 4{degrees}C, and milk (M) was used as a control. Peptides, amino acids, fatty acids, mono- and disaccharides, and their low molecular weight derivatives were evaluated. In total, 348 peptides, 37 amino acids, 25 fatty acids, and 23 mono- and disaccharides were identified in the products. Among them, 41 functional peptides, branch-chained amino acids (BCAA), orotic acid (vitamin B13), d-phenyllactic acid, 5-phenylvaleric acid and myo-inositol (vitamin B8) accumulated in fermented products during storage.

biochemistry↗

Mechanism of Curaxin-dependent Nucleosome Unfolding by FACT

Human FACT (FACT) is a multifunctional histone chaperone involved in transcription, replication and DNA repair. Curaxins are anticancer compounds that induce FACT- dependent nucleosome unfolding and trapping of FACT in the chromatin of cancer cells (c-trapping) through an unknown molecular mechanism. Here, we analyzed the effects of curaxin CBL0137 on nucleosome unfolding by FACT using spFRET and electron microscopy. By itself, FACT adopted multiple conformations, including a novel, compact, four-domain state in which the previously unresolved NTD of the SPT16 subunit of FACT was localized, apparently stabilizing a compact configuration. Multiple, primarily open conformations of FACT-nucleosome complexes were observed during curaxin-supported nucleosome unfolding. The structures of intermediates suggest "decision points" in the unfolding/folding pathway where FACT can either promote disassembly or assembly of nucleosomes, with the outcome possibly being influenced by additional factors. The data suggest novel mechanisms of nucleosome unfolding by FACT and c-trapping by curaxins.

cancer biology↗