Document Detail

Inhibition of dipeptidyl peptidase IV and xanthine oxidase by amino acids and dipeptides.
MedLine Citation:
PMID:  23768405     Owner:  NLM     Status:  In-Data-Review    
Xanthine oxidase (XO) and dipeptidyl peptidase IV (DPP-IV) inhibition by amino acids and dipeptides was studied. Trp and Trp-containing dipeptides (Arg-Trp, Trp-Val, Val-Trp, Lys-Trp and Ile-Trp) inhibited XO. Three amino acids (Met, Leu and Trp) and eight dipeptides (Phe-Leu, Trp-Val, His-Leu, Glu-Lys, Ala-Leu, Val-Ala, Ser-Leu and Gly-Leu) inhibited DPP-IV. Trp and Trp-Val were multifunctional inhibitors of XO and DPP-IV. Lineweaver and Burk analysis showed that Trp was a non-competitive inhibitor of XO and a competitive inhibitor of DPP-IV. Molecular docking with Autodock Vina was used to better understand the interaction of the peptides with the active site of the enzyme. Because of the non-competitive inhibition observed, docking of Trp-Val to the secondary binding sites of XO and DPP-IV is required. Trp-Val was predicted to be intestinally neutral (between 25% and 75% peptide remaining after 60min simulated intestinal digestion). These results are of significance for the reduction of reactive oxygen species (ROS) and the increase of the half-life of incretins by food-derived peptides.
Alice B Nongonierma; Catherine Mooney; Denis C Shields; Richard J Fitzgerald
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Publication Detail:
Type:  Journal Article     Date:  2013-03-07
Journal Detail:
Title:  Food chemistry     Volume:  141     ISSN:  0308-8146     ISO Abbreviation:  Food Chem     Publication Date:  2013 Nov 
Date Detail:
Created Date:  2013-06-17     Completed Date:  -     Revised Date:  -    
Medline Journal Info:
Nlm Unique ID:  7702639     Medline TA:  Food Chem     Country:  England    
Other Details:
Languages:  eng     Pagination:  644-53     Citation Subset:  IM    
Copyright Information:
Copyright © 2013 Elsevier Ltd. All rights reserved.
Department of Life Sciences and Food for Health Ireland (FHI), University of Limerick, Castletroy, Limerick, Ireland.
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