Potensi Peptida Bioaktif dari Protein Globulin 11S Biji Salvia hispanica L. sebagai Inhibitor α-Glukosidase secara in Silico

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.