Аннотация:The aim of this work was to design and characterize peptides based on the α-helices h1 and h2 ofthe ACE2 receptor, forming the interaction interface between the receptor-binding domain (RBD) of theSARS-CoV-2 S protein and the cellular ACE2 receptor. Monomeric and heterodimeric peptides connectedby disulfide bonds at different positions were synthesized. Solubility, RBD-binding affinity, and peptide heli-city were experimentally measured, and molecular dynamics simulation was performed in various solvents. Itwas established that the preservation of the helical conformation is a necessary condition for the binding ofpeptides to RBD. The peptides have a low degree of helicity and low affinity for RBD in water. Dimeric pep-tides have a higher degree of helicity than monomeric ones, probably due to the mutual inf luence of helices.The degree of helicity of the peptides in trifluoroethanol is the highest; however, for in vitro studies, the mostsuitable solvent is a water-ethanol mixture.