Properties and Activity of Peptide Derivatives of ACE2 Cellular Receptor and Their Interaction with SARS-CoV-2 S Protein Receptor-Binding Domain.

Autor: Sidorova MV; Chazov National Medical Research Center for Cardiology, Ministry of Health of the Russian Federation, Moscow, Russia., Bibilashvili RS; Chazov National Medical Research Center for Cardiology, Ministry of Health of the Russian Federation, Moscow, Russia., Avdeev DV; Chazov National Medical Research Center for Cardiology, Ministry of Health of the Russian Federation, Moscow, Russia., Kozhokar US; Chazov National Medical Research Center for Cardiology, Ministry of Health of the Russian Federation, Moscow, Russia., Palkeeva ME; Chazov National Medical Research Center for Cardiology, Ministry of Health of the Russian Federation, Moscow, Russia., Ovchinnikov MV; Chazov National Medical Research Center for Cardiology, Ministry of Health of the Russian Federation, Moscow, Russia., Molokoedov AS; Chazov National Medical Research Center for Cardiology, Ministry of Health of the Russian Federation, Moscow, Russia., Shirokov DA; Federal Research and Clinical Center of Physical Chemical Medicine, Federal Medical Biological Agency, Moscow, Russia.; Skryabin Moscow State Academy of Veterinary Medicine and Biotechnology, Moscow, Russia., Semyonova AV; Federal Research and Clinical Center of Physical Chemical Medicine, Federal Medical Biological Agency, Moscow, Russia., Uvarova VI; Chumakov Federal Scientific Center for Research and Development of Immune and Biological Products of the Russian Academy of Sciences (Institute of Poliomyelitis), Moscow, Russia., Kulyaev PO; Sirius University of Science and Technology, Sochi, Russia., Khvatov EV; Chumakov Federal Scientific Center for Research and Development of Immune and Biological Products of the Russian Academy of Sciences (Institute of Poliomyelitis), Moscow, Russia., Ignatova AA; Institute of Bioorganic Chemistry, Russian Academy of Sciences, Moscow, Russia., Feofanov AV; Lomonosov Moscow State University, Moscow, Russia., Osolodkin DI; Chumakov Federal Scientific Center for Research and Development of Immune and Biological Products of the Russian Academy of Sciences (Institute of Poliomyelitis), Moscow, Russia.; Sechenov First Moscow State Medical University (Sechenov University), Moscow, Russia., Porozov YB; Sirius University of Science and Technology, Sochi, Russia.; Sechenov First Moscow State Medical University (Sechenov University), Moscow, Russia., Kozlovskaya LI; Chumakov Federal Scientific Center for Research and Development of Immune and Biological Products of the Russian Academy of Sciences (Institute of Poliomyelitis), Moscow, Russia. kozlovskaya_li@chumakovs.su.; Sechenov First Moscow State Medical University (Sechenov University), Moscow, Russia. kozlovskaya_li@chumakovs.su., Ishmukhametov AA; Chumakov Federal Scientific Center for Research and Development of Immune and Biological Products of the Russian Academy of Sciences (Institute of Poliomyelitis), Moscow, Russia.; Sechenov First Moscow State Medical University (Sechenov University), Moscow, Russia., Parfyonova YV; Chazov National Medical Research Center for Cardiology, Ministry of Health of the Russian Federation, Moscow, Russia., Egorov AM; Chumakov Federal Scientific Center for Research and Development of Immune and Biological Products of the Russian Academy of Sciences (Institute of Poliomyelitis), Moscow, Russia.; Lomonosov Moscow State University, Moscow, Russia.
Jazyk: angličtina
Zdroj: Doklady. Biochemistry and biophysics [Dokl Biochem Biophys] 2022 Dec; Vol. 507 (1), pp. 237-241. Date of Electronic Publication: 2022 Dec 29.
DOI: 10.1134/S1607672922060126
Abstrakt: The aim of this work was to design and characterize peptides based on the α-helices h1 and h2 of the ACE2 receptor, forming the interaction interface between the receptor-binding domain (RBD) of the SARS-CoV-2 S protein and the cellular ACE2 receptor. Monomeric and heterodimeric peptides connected by disulfide bonds at different positions were synthesized. Solubility, RBD-binding affinity, and peptide helicity were experimentally measured, and molecular dynamics simulation was performed in various solvents. It was established that the preservation of the helical conformation is a necessary condition for the binding of peptides to RBD. The peptides have a low degree of helicity and low affinity for RBD in water. Dimeric peptides have a higher degree of helicity than monomeric ones, probably due to the mutual influence of helices. The degree of helicity of the peptides in trifluoroethanol is the highest; however, for in vitro studies, the most suitable solvent is a water-ethanol mixture.
(© 2022. The Author(s).)
Databáze: MEDLINE
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