In Silico Screening of a Bile Acid Micelle Disruption Peptide for Oral Consumptions from Edible Peptide Database.

Kento Imai,Kazunori Shimizu,Yuri Takeuchi,Hiroyuki Honda

doi:10.3390/foods10102496

Kento Imai, Kazunori Shimizu + Show 2 more

Open Access

https://doi.org/10.3390/foods10102496

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Abstract

Recently, many bioactive peptides have been identified using bioinformatics tools. Previously, our group developed a method to screen dual-functional peptides that have direct intestinal delivery with porous silica gel and bile acid micelle disruption. However, newly designed peptides were not found in any storage protein. Therefore, in this study, in silico screening was performed using a 350,000 edible peptide library consisting of 4- to 7-mer independent peptides. As an initial screening, all edible peptides were applied to the random forest model to select predicted positive peptides. For a second screening, the peptides were assessed for the possibility of intestinal delivery using a 3D color map. From this approach, three novel dual-functional peptides, VYVFDE, WEFIDF, and VEEFYC were identified, and all of them were derived from storage proteins (legumin, myosin, and 11S globulin). In particular, VEEFYCS, in which a serine residue (S) is added to VEEFYC, was assumed to be released by thermolysin from the 11S-globulin derived from Ginkgo biloba by LC-MS/MS analysis. VEEFYCS was found to have suitable direct intestinal delivery and bile acid micelle disruption activity.

Highlights

Bioactive peptides provide health benefits to consumers, and many bioactive peptides have been identified from protein sources such as milk, plant seed, and seafood, among others [1]
Some bile acid-binding peptides have been screened by the principal component analysis (PCA) model from a randomly designed peptide library, and ExPASy was utilized to identify the peptides which could be isolated by enzyme hydrolysis [9,10]
A set of 710 edible proteins was downloaded from BIOPEP-UWM, and sequences were divided into 4-mer, 5-mer, 6-mer, or 7-mer peptide fragments with one residue shift from the N-terminal, resulting in up to 350,000 independent peptides

Summary

Introduction

Bioactive peptides provide health benefits to consumers, and many bioactive peptides have been identified from protein sources such as milk, plant seed, and seafood, among others [1]. The basic approach to identify bioactive peptides proceeds as follows: protein extraction, isolation, enzymatic hydrolysis, peptide purification, and verification of bioactivity in chemically synthesized peptides [1,2]. This “classical” method is laborious and time-consuming due to the trial-and-error process [3]. Bile acid-binding peptides can act as suppressors of cholesterol absorption via disruption of bile acid micelles including cholesterol molecules, resulting in a lowering of cholesterol levels in blood Using this integrated approach, many bioactive peptides that could be isolated by enzyme hydrolysis have been identified within a short time

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Conclusion