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Inhibition of dipeptidyl peptidase IV and xanthine oxidase by amino acids and dipeptides

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dc.contributor.author Nongonierma, Alice B.
dc.contributor.author Mooney, Catherine
dc.contributor.author Shields, Denis C
dc.contributor.author Fitzgerald, Richard J.
dc.date.accessioned 2017-04-13T10:35:25Z
dc.date.available 2017-04-13T10:35:25Z
dc.date.issued 2013
dc.identifier.uri http://hdl.handle.net/10344/5709
dc.description peer-reviewed en_US
dc.description.abstract 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 60 min 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. (C) 2013 Elsevier Ltd. All rights reserved. en_US
dc.language.iso eng en_US
dc.publisher Elsevier en_US
dc.relation.ispartofseries Food Chemistry;141 (1), pp. 644-653
dc.relation.uri http://dx.doi.org/10.1016/j.foodchem.2013.02.115
dc.rights This is the author’s version of a work that was accepted for publication in Food Chemistry. Changes resulting from the publishing process, such as peer review, editing, corrections, structural formatting, and other quality control mechanisms may not be reflected in this document. Changes may have been made to this work since it was submitted for publication. A definitive version was subsequently published in Food Chemistry, 141 (1), pp. 644-653,http://dx.doi.org/10.1016/j.foodchem.2013.02.115 en_US
dc.subject dipeptidyl peptidase IV inhibitors en_US
dc.subject xanthine oxidase inhibitors en_US
dc.subject amino acids en_US
dc.subject dipeptides en_US
dc.subject milk en_US
dc.subject predictive modelling en_US
dc.title Inhibition of dipeptidyl peptidase IV and xanthine oxidase by amino acids and dipeptides en_US
dc.type info:eu-repo/semantics/article en_US
dc.type.supercollection all_ul_research en_US
dc.type.supercollection ul_published_reviewed en_US
dc.date.updated 2017-04-10T18:24:27Z
dc.description.version ACCEPTED
dc.identifier.doi 10.1016/j.foodchem.2013.02.115
dc.contributor.sponsor EI en_US
dc.contributor.sponsor SFI en_US
dc.relation.projectid CC20080001 en_US
dc.relation.projectid 08/IN.1/B1864 en_US
dc.rights.accessrights info:eu-repo/semantics/openAccess en_US
dc.internal.rssid 1443073
dc.internal.copyrightchecked Yes
dc.identifier.journaltitle Food Chemistry
dc.description.status peer-reviewed


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