Analyzing a dipeptide library to identify human dipeptidyl peptidase IV inhibitor

•The human dipeptidyl peptidase IV inhibitory effects of 337 dipeptides were analyzed.•Trp-Arg showed the highest inhibitory effect among dipeptides.•N-terminal amino acids of dipeptides play a dominant role in their inhibition intensities.•Five novel highly inhibitory dipeptides were discovered.•Th...

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Bibliographic Details
Published in:Food chemistry 2015-05, Vol.175, p.66-73
Main Authors: Lan, Vu Thi Tuyet, Ito, Keisuke, Ohno, Masumi, Motoyama, Takayasu, Ito, Sohei, Kawarasaki, Yasuaki
Format: Article
Language:English
Subjects:
Amino Acid Sequence
Animals
Dietary Proteins - analysis
Dietary Proteins - chemistry
Dipeptide
Dipeptides - analysis
Dipeptides - chemistry
Dipeptides - pharmacology
Dipeptidyl-Peptidase IV Inhibitors - analysis
Dipeptidyl-Peptidase IV Inhibitors - chemistry
Dipeptidyl-Peptidase IV Inhibitors - pharmacology
Functional food
Human dipeptidyl peptidase IV
Humans
Molecular Sequence Data
Peptide Library
Soybean Proteins - analysis
Soybean Proteins - chemistry
Type 2 diabetes
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Summary:•The human dipeptidyl peptidase IV inhibitory effects of 337 dipeptides were analyzed.•Trp-Arg showed the highest inhibitory effect among dipeptides.•N-terminal amino acids of dipeptides play a dominant role in their inhibition intensities.•Five novel highly inhibitory dipeptides were discovered.•The dataset provided novel insight into the development of functional food for type 2 diabetes. Human dipeptidyl peptidase IV (hDPPIV) inhibitors provide an effective strategy for the treatment of type 2 diabetes. Because certain peptides are known to act as hDPPIV inhibitors, a dataset of possible peptides with their inhibition intensities will facilitate the development of functional food for type 2 diabetes. In this study, we examined a total of 337 dipeptides with respect to their hDPPIV inhibitory effects. Amino acid residues at N-termini dominated their inhibition intensities. Particularly highly inhibitory dipeptides discovered included the following novel dipeptides: Thr-His, Asn-His, Val-Leu, Met-Leu, and Met-Met. Using our dataset, prime candidates contributing to the hDPPIV inhibitory effect of soy protein hydrolyzates were successfully identified. Possible dietary proteins potentially able to produce particularly highly hDPPIV inhibitory peptides are also discussed on the basis of the dataset.
ISSN:0308-8146
1873-7072
DOI:10.1016/j.foodchem.2014.11.131