Prediksi Peptida Bioaktif Dari Protein Globulin 13S dan Albumin Biji Fagopyrum esculentum Terhadap Angiotensin Converting Enzyme Secara In Siliko

Abstract

Background: Hypertension is one of the most common cardiovascular diseases and requires long-term treatment with synthetic drugs, which carry the risk of side effects. Therefore, the use of bioactive peptides derived from plant sources such as buckwheat (Fagopyrum esculentum) is an alternative as an Angiotensin Converting Enzyme (ACE) receptor inhibitor. Objective: This study aims to predict the potential of bioactive peptides resulting from the hydrolysis of 13S globulin and albumin proteins from Fagopyrum esculentum seeds using pepsin enzyme as an Angiotensin Converting Enzyme (ACE) inhibitor in silico. Methods: This study was conducted by examining predictions of biological activity, physicochemical properties, pharmacokinetics, allergenicity, and toxicity, as well as molecular docking simulations on ACE receptors. Result: Based on the research results, out of 161 peptides obtained from hydrolysis, there were 121 13S globulin peptides and 40 albumin peptides that had the potential to be ACE inhibitors. Some of the peptides met Lipinski's Rule of Five criteria and pharmacokinetic parameters, while others had non-toxic and non-allergenic properties. The binding affinity values from the docking results ranged from -4,39 to -9,37 kcal/mol, with the IPSPA peptide showing the best binding affinity value of -7,83 kcal/mol and important amino acid residue interactions similar to the native ligand and comparator. Conclusion: Peptides resulting from the hydrolysis of 13S globulin protein and albumin from Fagopyrum esculentum seeds using pepsin enzyme have potential as a source of bioactive peptides that inhibit ACE in silico.