Prospecting in silico antibacterial activity of a peptide from trypsin inhibitor isolated from tamarind seed

Abstract

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.

Graphical Abstract

Keywords:

• Protease inhibitor
• antimicrobial peptides
• molecular dynamics simulation

Disclosure statement

No potential conflict of interest was reported by the author(s).

Additional information

Funding

This work was supported for scholarship and payment of fees by the Coordenação de Aperfeiçoamento de Pessoal de Nível Superior (Finance Code 001 – CAPES). The research leading to these results received funding from the European Union’s H2020 Research and Innovation Programme under the Maria Sklodowska-Curie grant agreement N 778388 [H2020 MSCA-RISE-2017 project Food for Diabetes and Cognition (FODIAC), and grant agreement N 713640 (MSCA-2015-COFUND_FP)].