In Silico Analysis of Bioactive Peptides Released from Giant Grouper (Epinephelus lanceolatus) Roe Proteins Identified by Proteomics Approach.

Fenny Crista A Panjaitan,Honey Lyn R Gomez,Yu-Wei Chang

doi:10.3390/molecules23112910

Fenny Crista A Panjaitan, Honey Lyn R Gomez + Show 1 more

Open Access

https://doi.org/10.3390/molecules23112910

Copy DOI

Abstract

Major proteins contained in dried giant grouper roe (GR) such as vitellogenin (from Epinephelus coioides; NCBI accession number: AAW29031.1), apolipoprotein A-1 precursor (from Epinephelus coioides; NCBI accession number: ACI01807.1) and apolipoprotein E (from Epinephelus bruneus; NCBI accession number: AEB31283.1) were characterized through compiled proteomics techniques (SDS-PAGE, in-gel digestion, mass spectrometry and on-line Mascot database analysis). These proteins were subjected to in silico analysis using BLAST and BIOPEP-UWM database. Sequence similarity search by BLAST revealed that the aligned vitellogenin sequences from Epinephelus coioides and Epinephelus lanceolatus share 70% identity, which indicates that the sequence sample has significant similarity with proteins in sequence databases. Moreover, prediction of potential bioactivities through BIOPEP-UWM database resulted in high numbers of peptides predominantly with dipeptidyl peptidase-IV (DPP-IV) and angiotensin-I-converting enzyme (ACE-I) inhibitory activities. Pepsin (pH > 2) was predicted to be the most promising enzyme for the production of bioactive peptides from GR protein, which theoretically released 82 DPP-IV inhibitory peptides and 47 ACE-I inhibitory peptides. Overall, this work highlighted the potentiality of giant grouper roe as raw material for the generation of pharmaceutical products. Furthermore, the application of proteomics and in silico techniques provided rapid identification of proteins and useful prediction of its potential bioactivities.

Highlights

Bioactive peptides such as antihypertensive [1,2,3] and anti-diabetic peptides [4,5] are widely observed due to their good potential as pharmaceutical products, for human health enhancement
Singh et al [10] reported that dipeptidyl peptidase IV (DPP-IV) cleaves incretin hormones such as glucagon-like peptide 1 (GLP-1) and glucose-dependent insulinotropic peptide (GIP), resulting in diabetes mellitus type 2 (DM2)
The objectives of this study are to identify the major proteins contained in giant grouper roe using a proteomics approach; to demonstrate in silico analysis for the prediction of angiotensin-I-converting enzyme (ACE-I) and DPP-IV inhibitory peptides encrypted in the protein sequence of giant grouper roe; and to screen proteases based on their capacity to release huge number of bioactive peptides through enzymatic hydrolysis simulation

Summary

Introduction

Bioactive peptides such as antihypertensive [1,2,3] and anti-diabetic peptides [4,5] are widely observed due to their good potential as pharmaceutical products, for human health enhancement. Hypertension is one of the major risk factors causing cardiovascular diseases, and generally occurs with obesity, pre-diabetes and atherosclerosis [6,7,8]. Diabetes mellitus type 2 (DM2) commonly occurs worldwide, and is one of the prime causes of death. Singh et al [10] reported that dipeptidyl peptidase IV (DPP-IV) cleaves incretin hormones such as glucagon-like peptide 1 (GLP-1) and glucose-dependent insulinotropic peptide (GIP), resulting in DM2. Some synthetic therapeutic drugs have been developed to treat hypertension and DM2; the majority of them are considered unsafe due to the side effects

Objectives

Methods

Results

Discussion

Conclusion