Doklady. Biochemistry and biophysics · 2022
Properties and Activity of Peptide Derivatives of ACE2 Cellular Receptor and Their Interaction with SARS-CoV-2 S Protein Receptor-Binding Domain.
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Sidorova M V, Bibilashvili R S, Avdeev D V, Kozhokar U S, Palkeeva M E, Ovchinnikov M V, Molokoedov A S, Shirokov D A, Semyonova A V, Uvarova V I, Kulyaev P O, Khvatov E V, Ignatova A A, Feofanov A V, Osolodkin D I, Porozov Yu B, Kozlovskaya L I, Ishmukhametov A A, Parfyonova Ye V, Egorov A M
Аннотация
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.