Novel octapeptide containing the RGD sequence as a potential anti-SARS-CoV-2 agent: design, synthesis, and theoretical studies.
Reiner Lemos, Orlando Ortiz, Luis Almagro, Kamil Makowski, Hortensia Rodríguez, Fernando Albericio, Margarita Suarez
Abstract
Open AccessThe design of peptide-based inhibitors targeting cell receptors represents a promising strategy in the development of antiviral agents. In this study, a novel octapeptide containing the RGD sequence was rationally designed to explore its potential interaction with integrins. The peptide was functionalized with a malonic moiety to enhance its binding capabilities and potential bioactivity. Conformational and physicochemical properties were evaluated using DFT-PBEh-3c calculations. Molecular docking studies revealed favorable interactions with the integrin α5β1, including coordination with the Mg²⁺ ion at the active site. The peptide was successfully synthesized via Fmoc-based solid-phase peptide synthesis (SPPS) and fully characterized by NMR, IR, MS, and RP-HPLC.