Structural insights and molecular dynamics into the inhibitory mechanism of a kunitz-type trypsin inhibitor from tamarindus indica L

• Autor(a) principal: Maciel, Bruna Leal Lima
• Data de Publicação: 2021
• Outros Autores: Medeiros, Amanda Fernandes de, Souza, Beatriz Blenda Pinheiro de, Coutinho, Lucas Pinheiro, Murad, Aline Melro, Santos, Paula Ivani Medeiros dos, Monteiro, Norberto de Kássio Vieira, Santos, Elizeu Antunes dos, Morais, Ana Heloneida de Araújo
• Tipo de documento: Artigo
• Idioma: eng
• Título da fonte: Repositório Institucional da UFRN
• Texto Completo: https://repositorio.ufrn.br/handle/123456789/57449; http://dx.doi.org/10.1080/14756366.2021.1876686
• topic: Tamarind; Antitryptic; Homology modelling; Computational methods; Protein-protein interaction

Trypsin inhibitors from tamarind seed have been studied in vitro and in preclinical studies for the treatment of obesity, its complications and associated comorbidities. It is still necessary to fully understand the structure and behaviour of these molecules. We purifed this inhibitor, sequenced de novo by MALDI-TOF/ TOF, performed its homology modelling, and assessed the interaction with the trypsin enzyme through molecular dynamics (MD) simulation under physiological conditions. We identified additional 75 amino acid residues, reaching approximately 72% of total coverage. The four best conformations of the best homology modelling were submitted to the MD. The conformation n287 was selected considering the RMSD analysis and interaction energy (–301.0128 kcal.mol1 ). Residues Ile (54), Pro (57), Arg (59), Arg (63), and Glu (78) of pTTI presented the highest interactions with trypsin, and arginine residues were mainly involved in its binding mechanism. The results favour bioprospecting of this protein for pharmaceutical health applications