Journal
PEPTIDES
Volume 54, Issue -, Pages 166-170Publisher
ELSEVIER SCIENCE INC
DOI: 10.1016/j.peptides.2014.01.027
Keywords
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Funding
- JSPS KAKENHI [2370139]
- Fuji Foundation for Protein Research
- Grants-in-Aid for Scientific Research [23780139] Funding Source: KAKEN
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Human dipeptidyl peptidase IV (hDPPIV, alternative name: CD26) inhibitors provide an effective strategy for the treatment of type 2 diabetes. Recently, our research group discovered a non substrate-mimic inhibitory dipeptide, Trp-Arg, by the systematic analysis of a dipeptide library. In the present study, a tripeptide library Trp-Arg-Xaa (where Xaa represents any amino acid) was analyzed to investigate the interactions of peptidergic inhibitors with hDPPIV. Trp-Arg-Glu showed the highest inhibitory effect toward hDPPIV (Ki= 130 p,M). All of the tested 19 Trp-Arg-Xaa tripeptides showed unique uncompetitivetype inhibition. The inhibition mechanism of Trp-Arg-Xaa is discussed based on the crystal structure of hDPPIV. The information obtained by this study suggests a novel concept for developing hDPPIV inhibitory peptides and drugs. (c) 2014 Elsevier Inc. All rights reserved.
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