To date, a large body of data has been accumulated on the biological activity of a low-toxic natural glycoside, glycyrrhizic acid (GA), but the mechanism of its action at the molecular level has not been fully studied. Expanding knowledge about the spectrum of cellular protein targets of GA contributes to understanding new features of pharmacodynamics. The aim of the work was the experimental identification of a tissue-specific spectrum of protein molecules interacting with GA in a model system.
View Article and Find Full Text PDFVirus-neutralizing peptides (VNPs) emerged as promising antiviral drug candidates with unprecedented specificity and cost-effectiveness during the recent COVID-19 pandemic. However, limited avidity, lack of effector functions, short circulatory half-life, and restricted administration routes make them inferior compared to neutralizing antibodies. To address these constraints, a potent VNP that targets the SARS-CoV-2 S protein is combined with Barnase, a highly active RNA-cleaving enzyme from Bacillus amyloliquefaciens.
View Article and Find Full Text PDFRenalase (RNLS) is a protein playing different roles inside and outside cells. A 20-mer synthetic peptide corresponding to the human RNLS amino acid sequence 220-239 (RP220) exhibits a number of pharmacologically attractive activities in vitro and in vivo and can bind to many renal intracellular proteins. The RP220 sequence contains several cleavage sites for extracellular and circulating proteases.
View Article and Find Full Text PDFThe interaction of inactivated poliovirus vaccine strains with oriented antibodies immobilized to protein A via Fc fragments has been investigated. Using an SPR biosensor, the kinetic and equilibrium parameters of the interaction of vaccine attenuated polioviruses of the Sabin strains type 1 and type 2, inactivated by various methods were determined. The strongest interaction was observed between polyclonal antibodies to Sabin strain type 2 poliovirus and Sabin strain type 2 poliovirus inactivated with β-propiolactone, KD = 1.
View Article and Find Full Text PDFInt J Mol Sci
February 2024
Dehydroepiandrosterone (DHEA), a precursor of steroid sex hormones, is synthesized by steroid 17-alpha-hydroxylase/17,20-lyase (CYP17A1) with the participation of microsomal cytochrome b5 (CYB5A) and cytochrome P450 reductase (CPR), followed by sulfation by two cytosolic sulfotransferases, SULT1E1 and SULT2A1, for storage and transport to tissues in which its synthesis is not available. The involvement of CYP17A1 and SULTs in these successive reactions led us to consider the possible interaction of SULTs with DHEA-producing CYP17A1 and its redox partners. Text mining analysis, protein-protein network analysis, and gene co-expression analysis were performed to determine the relationships between SULTs and microsomal CYP isoforms.
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