| dc.description.abstract | Background: Diabetes mellitus was a metabolic disease characterized by chronic
hyperglycemia. α-Glucosidase inhibitors were one therapeutic approach to
controlling postprandial blood glucose levels. Bioactive peptides from the 11S
globulin protein of Salvia hispanica L. seeds had shown potential as natural
therapeutic agents in silico.
Objective: This study aimed to predict that the potential bioactive peptides derived
from the 11S globulin protein of Salvia hispanica L. seeds had antidiabetic activity
by inhibiting α-glucosidase in silico
Methods: The study was conducted through several stages including peptide
cleavage simulation using PeptideCutter, prediction of peptide bioactivity using
Peptide Ranker, prediction of peptide biological activity with Biopep and PASS
Online, prediction of physicochemical properties with Lipinski’s Rule of Five,
pharmacokinetic properties with SwissADME, toxicity with ToxinPred,
allergenicity with Allertop, and molecular docking on α-glucosidase receptors.
Results: The study showed that 49 peptides were predicted to have activity in
lowering blood glucose levels, 47 peptides had high bioactivity, 31 peptides met
the physicochemical parameters of Lipinski’s Rule of Five, 19 peptides met the
pharmacokinetic parameters, 174 peptides were non-toxic, and 83 peptides were
non-allergenic. Docking results showed binding affinity values between peptides
and α-glucosidase inhibitors ranging from -3.280 to -6.876; the binding affinity
value for the native ligand was -3.745; and the binding affinity value for the
comparator miglitol was -4.421.
Conclusion: The results identified peptides capable of inhibiting α-glucosidase,
specifically the peptide TF with a binding affinity value of -6.137 obtained through
hydrolysis using pepsin enzyme from the ExPASy website, which interacted with
α-glucosidase via hydrogen bonds and hydrophobic interactions at the amino acid
residues Leu756, His742, and Thr764. | en_US |
