Antihypertensive Activity of Peptides Derived from Toman Fish Albumin (Channa micropeltes): In-silico Angiotensin-Converting Enzyme Inhibitory Study.

Abstract

The peptides from protein hydrolysis can be as bioactive peptides. Currently, the process of protein hydrolysis can be done in-silico technique, an alternative to bioactive peptide identification more effectively and efficiently. This study aims to predict bioactive peptides in-silico technique of albumin hydrolysis from Toman Fish (Channa micropeltes), which had the potential as an antihypertensive drug. Toman fish albumin sequence (A0A191TFW5) was obtained from the UniProt database. The identification of bioactive peptides was performed by simulating enzymatic hydrolysis with three human digestive enzymes: trypsin, chymotrypsin, and pepsin. The hydrolysis simulation of albumin was conducted using the ExPASy PeptideCutter program. The generated peptides’ potential activities, solubility, and ADMET (absorption, distribution, metabolism, excretion, and toxicity) properties were predicted using various online prediction tools. Molecular docking was performed on the bioactive peptides to determine the Gibbs free energy (∆G) and to illustrate the interaction between the bioactive peptides and the active site of the Angiotensin Converting Enzyme (ACE) as a comparison was used captopril which was a commercial ACE inhibitor. The results showed that bioactive peptide candidates were AI, VL and LVP. These peptides were potentially a candidate for alternative antihypertensive drugs.