Banca de QUALIFICAÇÃO: LARISSA AIDA LEMOS DE SOUZA

Uma banca de QUALIFICAÇÃO de MESTRADO foi cadastrada pelo programa.
STUDENT : LARISSA AIDA LEMOS DE SOUZA
DATE: 05/12/2024
TIME: 09:00
LOCAL: Sala de Reuniões do Departamento de Nutrição – UFRN
TITLE:

EVALUATION OF THE EFFECT OF TRYPSIN INHIBITOR ISOLATED FROM TAMARIND SEEDS, HYDROLYZED OR NOT, ON α-AMYLASE: AN IN VITRO AND IN SILICO STUDY

KEY WORDS:

Diabetes mellitus; protease inhibitors; bioactive peptides; molecular docking; molecular dynamics

PAGES: 68
BIG AREA: Ciências da Saúde
AREA: Nutrição
SUMMARY:

Among the main complications resulting from obesity, type 2 Diabetes Mellitus (DM2) stands out, which is a metabolic disorder in which there is persistent hyperglycemia. Therefore, it is necessary to find alternatives for the control of DM2 and among them, inhibitors of enzymes involved in the process of carbohydrate digestion appear as a possibility in glycemic control. The present study aimed to evaluate the effect of the trypsin inhibitor isolated from tamarind seed (Tamarindus indica L.) (ITT) hydrolyzed or not on α-amylase. After confirmation of the obtaining and characterization of the ITT, the in vitro inhibitory activity of ITT against α-amylase was analyzed. Then, the interaction of the theoretical ITT (ITTp 56/287) and some of its derived peptides with α-amylase was also evaluated in silico and their functional properties were evaluated. ITT showed 100% antitryptic activity and a molecular mass of approximately 21 kDa. The results of in vitro inhibition of α-amylase showed an inhibitory activity higher than 37%. These results were corroborated by computational analyses, which showed the strong interaction of the ITTp 56/287 complex with the enzyme, as well as its derived peptides. The RMSD (up to 0.4 nm) and RMFS (up to 0.4 nm) analyses showed low flexibility of the tested peptides, i.e., good stability. The potential energy of interaction (PEI) analysis showed < -550 kJ for the candidates, confirming the previous analyses. Furthermore, regarding the bioactive potential, it was observed that these candidates showed good stability, long half-life and bioactivity in an intestinal simulation environment. In short, according to the sum of findings of this study, it revealed the peptides, with the amino acid sequences, DTVHDTDGQVPL and TIAPACAPKPAR as candidate peptides that could be tested in in vitro and preclinical studies, and later clinical studies, for action against α-amylase, and consequently hypoglycemic effect, and could become an alternative in the treatment of DM2.

COMMITTEE MEMBERS:
Presidente - 2578619 - ANA HELONEIDA DE ARAUJO MORAIS
Externa à Instituição - ANNA BEATRIZ SANTANA LUZ - UFBA
Externo ao Programa - 1959889 - DAVI SERRADELLA VIEIRA - nullExterno à Instituição - NORBERTO DE KASSIO VIEIRA MONTEIRO - UFC