Beilstein J. Nanotechnol. 2022, 13, 699–711. https://doi.org/10.3762/bjnano.13.62
Supporting Information features previously reported antiviral activities of APD peptides (Table S1); molecular docking scores of the 104 peptides (Table S2); Ligplot+ diagrams of the hydrogen bonds and hydrophobic interactions between ACE2 and the SARS-CoV-2 RBD (Figure S1); distribution of electrostatic potential on the surface of APD peptide candidates docked to the SARS-CoV-2 RBD (Figure S2); secondary structure, docking, and distribution of electrostatic charges of aligned peptides (Figure S3); physicochemical properties, hydrogen bonds, and hydrophobic interactions of the peptide candidates against SARS-CoV-2 (Table S3); principal docking regions of screened APD and lysozyme peptides against the SARS-CoV-2 RBD (Figure S4); immunogenicity analysis of peptides against human MHC I to determine the number of alleles with IC50 < 50 nM and IC50 < 500 nM (Table S4); and the contact areas of peptides docked to SARS-CoV-2.
Supporting Information File 1: Additional experimental data. | ||
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