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In Silico approaches applied to the study of peptide analogs of ile-pro-ile in relation to their dipeptidyl peptidase IV inhibitory properties

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dc.contributor.author Nongonierma, Alice B.
dc.contributor.author Dellafiora, Luca
dc.contributor.author Paolella, Sara
dc.contributor.author Galaverna, Gianni
dc.contributor.author Cozzini, Pietro
dc.contributor.author Fitzgerald, Richard J.
dc.date.accessioned 2018-07-03T08:49:38Z
dc.date.available 2018-07-03T08:49:38Z
dc.date.issued 2018
dc.identifier.uri http://hdl.handle.net/10344/6935
dc.description peer-reviewed en_US
dc.description.abstract Inhibition of dipeptidyl peptidase IV (DPP-IV) may be exploited to maintain the incretin effect during the postprandial phase. As a result, glycemic regulation and energy homeostasis may be improved. Food protein-derived peptides have been identified as natural agents capable of inhibiting DPP-IV. Ile-Pro-Ile is the most potent DPP-IV inhibitory peptide identified to date. A minimum analog peptide set approach was used to study peptide analogs of Ile-Pro-Ile. The DPP-IV half maximal inhibitory concentration (IC50) values of the 25 peptides evaluated ranged from 3.9 ± 1.0 μM (Ile-Pro-Ile) to 247.0 ± 32.7 μM (Phe-Pro-Phe). The presence of Pro at position 2 of tripeptides was required to achieve high DPP-IV inhibition. Most peptides behaved as competitive inhibitors of DPP-IV with the exception of peptides with a N-terminal Trp, which were mixed-type inhibitors. While possessing the structure of preferred DPP-IV substrates, most peptides studied were particularly stable during 30 min incubation with DPP-IV. Molecular docking revealed that Ile-Pro-Ile and its peptide analogs interacted in a very similar manner with the active site of DPP-IV. In addition, no correlation was found between the Hydropathic INTeraction score and the DPP-IV IC50 values of the peptides studied. This outcome suggests that free energy may not be directly responsible for enzyme inhibition by the peptides. Finally, novel DPP-IV inhibitory peptides were identified using the strategy employed herein. These results may be relevant for the development of food protein-derived peptides with serum glucose lowering and food intake regulatory properties in humans. en_US
dc.language.iso eng en_US
dc.publisher Frontiers Media en_US
dc.relation.ispartofseries Frontiers in Endocrinology;9;Article 329
dc.rights First published by Frontiers Media in Frontiers in Endocrinology 2018 en_US
dc.subject dipeptidyl peptidase IV inhibition en_US
dc.subject Ile-Pro-Ile (diprotin A) en_US
dc.subject bioactive peptides en_US
dc.subject peptide analogs en_US
dc.subject design of experiments en_US
dc.subject quantitative structure activity relationship en_US
dc.subject molecular docking en_US
dc.title In Silico approaches applied to the study of peptide analogs of ile-pro-ile in relation to their dipeptidyl peptidase IV inhibitory properties 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.identifier.doi 10.3389/fendo.2018.00329
dc.identifier.doi 10.3390/md16060176
dc.contributor.sponsor EI en_US
dc.relation.projectid TC2013-0001 en_US
dc.rights.accessrights info:eu-repo/semantics/openAccess en_US


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