Prospecting in silico antibacterial activity of a peptide from trypsin inhibitor isolated from tamarind seed
| Autor: | Gerciane Silva de Oliveira, Amanda Maria de Souza Nascimento, Anna Beatriz Santana Luz, Ana Júlia Felipe Camelo Aguiar, Mayara Santa Rosa Lima, Lídia Leonize Rodrigues Matias, Isabel Rodríguez Amado, Thais Souza Passos, Karla Suzane Florentino da Silva Chaves Damasceno, Norberto de Kássio Vieira Monteiro, Susana Margarida Gomes Moreira, Lorenzo Pastrana, Ana Heloneida de Araújo Morais |
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| Rok vydání: | 2022 |
| Předmět: | |
| Zdroj: | Journal of Enzyme Inhibition and Medicinal Chemistry. 38:67-83 |
| ISSN: | 1475-6374 1475-6366 |
| DOI: | 10.1080/14756366.2022.2134997 |
| Popis: | Bacterial infections have become a global concern, stimulating the growing demand for natural and biologically safe therapeutic agents with antibacterial action. This study was evaluated the genotoxicity of the trypsin inhibitor isolated from tamarind seeds (TTI) and the antibacterial effect of TTI theoric model, number 56, and conformation number 287 (TTIp 56/287) and derived peptides in silico. TTI (0.3 and 0.6 mg.mL−1) did not cause genotoxicity in cells (p > 0.05). In silico, a greater interaction of TTIp 56/287 with the Gram-positive membrane (GP) was observed, with an interaction potential energy (IPE) of −1094.97 kcal.mol−1. In the TTIp 56/287-GP interaction, the Arginine, Threonine (Thr), and Lysine residues presented lower IPE. In molecular dynamics (MD), Peptidotrychyme59 (TVSQTPIDIPIGLPVR) showed an IPE of −518.08 kcal.mol−1 with the membrane of GP bacteria, and the Thr and Arginine residues showed the greater IPE. The results highlight new perspectives on TTI and its derived peptides antibacterial activity. |
| Databáze: | OpenAIRE |
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