Morais, Ana Heloneida de AraújoChaves, Rose de Paiva2024-07-092024-07-092024-06-03CHAVES, Rose de Paiva. Investigação do inibidor de tripsina de sementes de tamarindo (Tamarindus indica L.) como potencial agente terapêutico no Diabetes Mellitus: um estudo in silico sobre a interação com a α-amilase. Orientadora: Ana Heloneida de Araújo Morais. 2024. 41 f. Trabalho de Conclusão de Curso (Graduação em Nutrição) - Departamento de Nutrição, Universidade Federal do Rio Grande do Norte, Natal, 2024.https://repositorio.ufrn.br/handle/123456789/58723Tamarind seed trypsin inhibitor (Tamarindus indica L.) (ITT) has a variety of therapeutic effects in preclinical studies, and its hypoglycemic action has been shown in some of these studies. However, it is not yet known whether ITT inhibits enzymes involved in the carbohydrate digestion process, such as α-amylase. The objective of this study was to evaluate the in silico interaction between the theoretical amino acid sequences of ITT [model number 56, conformation number 287 (ITTp 56/287)] and pig α-amylase (PDB ID 1DHK). To this end, ClustalW2 was initially aligned between the ITTp 56/287 sequence and the three α-amylase inhibitor sequences most described in the literature RCSB PDB (PDB: Protein Data Bank). Then, the sequences were compared by similarity and the main conserved amino acid residues were identified. Finally, molecular docking was performed for the analysis of interaction prediction through the HDOCK server. The highest percentage of identity occurred between the α-amylase inhibitor (ID 1AVA_2) and ITTp 56/287, with 29.94%. When ITTp 56/287 was aligned with the α-amylase inhibitor with the highest identity, conserved amino acid residues were identified, including tyrosine (Y), lysine (K) and arginine (R), but they were not related to the active site of the α-amylase enzyme. Molecular docking showed high potential for interaction between ITTp 56/287 and α-amylase (docking score -234.30; Confidence Score 0.8437; Ligand RMSD 53.98), and 13 amino acids of ITTp 56/287 were identified with a smaller angle of interaction with α-amylase, among them serine (S), leucine (L), glutamic acid (E) and R. It is suggested, considering the in silico results, that ITTp has the potential to inhibit α-amylase in vitro and that it probably presents a non-competitive mechanistic because it does not interact in silico with the residues of the active site of the α-amylase used in this study. However, more studies will be needed for this new hypothesis to be confirmed.Attribution-NonCommercial-NoDerivs 3.0 Brazilhttp://creativecommons.org/licenses/by-nc-nd/3.0/br/Inibidor de proteaseInibidor de α-amilaseDocking molecularProtease inhibitorα-amylase inhibitorMolecular dockingbachelorThesisCNPQ::CIENCIAS DA SAUDE::NUTRICAO::BIOQUIMICA DA NUTRICAO