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Inhibition of dipeptidyl peptidase IV (DPP-IV) by tryptophan containing dipeptides

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dc.contributor.author Nongonierma, Alice B.
dc.contributor.author Fitzgerald, Richard J.
dc.date.accessioned 2017-04-13T09:01:45Z
dc.date.available 2017-04-13T09:01:45Z
dc.date.issued 2013
dc.identifier.uri http://hdl.handle.net/10344/5707
dc.description peer-reviewed en_US
dc.description.abstract Twenty seven Trp containing dipeptides were evaluated for their ability to inhibit dipeptidyl peptidase IV (DPP-IV), a key enzyme involved in incretin hormone processing. Novel DPP-IV inhibitors were identified comprising of three potent dipeptides (Trp-Arg, Trp-Lys and Trp-Leu) with half maximum inhibitory concentration (IC50 values) < 45 μM. With the exception of Leu-Trp which was ~20 times less potent than Trp-Leu, their reverse peptide did not inhibit DPP-IV. Trp-Asp was the only peptide studied herein with an N terminal Trp residue which was not a DPP-IV inhibitor. Phosphorylation resulted in an increase in DPP-IV IC50, giving values of 482.1 ± 12.9 and >11,000 μM for Trp-Thr and Trp-pThr, respectively. The mode of inhibition of these peptides was studied using Lineweaver and Burk kinetic analysis, which showed both competitive and non-competitive modes of inhibition depending on the peptide sequence. This suggested binding of the peptide inhibitors to different locations on DPP-IV. In silico analysis of the milk proteome revealed that some of the DPP-IV inhibitors identified herein may be released from milk proteins following enzymatic digestion. The results are relevant to understanding the mechanism(s) involved in DPP-IV inhibition by short peptides. This in turn may dictate a more targeted approach for the release of potent peptides from milk proteins with the view of developing biofunctional hydrolysates for the management of type 2 diabetes. en_US
dc.language.iso eng en_US
dc.publisher Royal Society of Chemistry en_US
dc.relation.ispartofseries Food and Function;4, pp. 1843-1849
dc.relation.uri http://dx.doi.org/10.1039/c3fo60262a
dc.rights Personal use of this material is permitted. Permission from Royal Society of Chemistry must be obtained for all other uses en_US
dc.subject dipeptidyl peptidase IV inhibitors en_US
dc.subject tryptophan en_US
dc.subject milk en_US
dc.subject type 2 diabetes en_US
dc.title Inhibition of dipeptidyl peptidase IV (DPP-IV) by tryptophan containing 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 2017-04-10T18:23:45Z
dc.description.version ACCEPTED
dc.identifier.doi 10.1039/c3fo60262a
dc.contributor.sponsor EI en_US
dc.relation.projectid CC20080001 en_US
dc.rights.accessrights info:eu-repo/semantics/openAccess en_US
dc.internal.rssid 1555966
dc.internal.copyrightchecked Yes
dc.identifier.journaltitle Food & Function
dc.description.status peer-reviewed


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