Uji In Silico Peptida Bioaktif dari Protein Globulin 13S dan Albumin Biji Fagopyrum esculentum Terhadap Dipeptidyl Peptidase-IV

Abstract

Background: Diabetes mellitus is a disease of blood glucose metabolism disorders. DM drugs that inhibit DPP-IV are at risk of causing side effects so that alternative natural treatments are needed. Buckwheat seeds are rich in proteins that are known to lower blood glucose. Objective: Predicting that protein hydrolysate of 13S globulin and albumin of Fagopyrum esculentum seeds have antidiabetic activity by inhibiting Dipeptidyl Peptidase-IV in silico. Method: Proceeded through peptide cleavage using Expasy and Biopep, analysis of bioactive peptide potential using Peptide Ranker, biological activity prediction using Biopep and PASS Online, physicochemical using Lipinski's Rule of Five, pharmacokinetics using SwissADME, toxicity using ToxinPred, allergenicity using AllerTOP, method validation, and molecular docking. Results: There are 76 13S globulin peptides and 32 albumin peptides were obtained from cleavage, 20 13S globulin peptides and 8 albumin peptides were potential bioactive peptides, 41 13S globulin peptides and 18 albumin peptides were predicted to have antidiabetic activity, 13 13S globulin peptides and 6 albumin peptides met Lipinski's Rule, 8 13S globulin peptides and 2 albumin peptides met pharmacokinetic parameters, 76 13S globulin peptides and 30 albumin peptides were non-toxic, and 43 13S globulin peptides and 23 albumin peptides were non allergen. The method validation yielded RMSD 0,5089Å, molecular docking results showed binding affinity of 13S globulin peptides ranging from -5,3337 to -7,9740 and binding affinity of albumin peptides ranging from -5,2660 to -7,6494, 26 13S globulin peptides and 5 albumin peptides are having binding affinity lower than the comparator and amino acid residue similarity with the native ligand and comparator Saxagliptin. Conclusion: Peptides from 13S globulin and albumin of Fagopyrum esculentum seeds exhibited antidiabetic activity, with test results showing that each peptide has inhibitory activity against Dipeptidyl Peptidase-IV in silico.