Restraint of VP1 Protein of Foot and Mouth Disease Virus using Specific Antiviral Peptides: an in Silico Investigation

• Published in: Archives of Razi Institute Vol. 78; no. 5; pp. 1483 - 1494
• Main Authors: Ali, Forouharmehr, Narges, Nazifi, Amin, Jaydari
• Format: Journal Article
• Language: English
• Published: Iran 01.10.2023
• Subjects: Animals; Antiviral Agents - pharmacology; Foot-and-Mouth Disease; Foot-and-Mouth Disease Virus; Molecular Docking Simulation; Peptides - metabolism; Peptides - pharmacology; Foot and mouth disease; In Silico; Antimicrobial Peptide; VP1
• ISSN: 0365-3439; 2008-9872
• DOI: 10.32592/ARI.2023.78.5.1483

Foot and mouth diseases are among the important threats in the animal husbandry industry which lead to huge economic losses. In this regard, the current project aimed to inhibit the VP1 protein of foot and mouth disease viruses using specific peptides. For this purpose, a wide range of potential antiviral peptides were collected from the database. Physicochemical properties, hydrophobicity/hydrophilicity, and solubility properties of potential antiviral peptides were investigated using reliable servers. Afterward, the tertiary structures of the selected peptides along with the VP1 protein were modeled by the I-TASSER server. Moreover, interactions between VP1 protein and selected antiviral peptides were investigated using the ClusPro 2.0 server. Finally, the outputs of molecular docking were assessed by LigPlot+ and visualized by PyMol software. The results revealed that , , , , , , , , and peptides with a hydrophobicity value of > 30 were soluble with positive instability index and positive net charge. Moreover, the results of the molecular docking process demonstrated that and peptides could strongly inhibit the VP1 protein using 10 hydrogen bonds. Therefore, these two peptides, which had the most hydrogen bonds, were introduced as the best anti-foot and mouth disease virus peptides to apply.