Identification and characterisation of peptides from a boarfish (Capros aper) protein hydrolysate displaying in vitro dipeptidyl peptidase-IV (DPP-IV) inhibitory and insulinotropic activity

Pádraigín A. Harnedy-Rothwell, Chris M. McLaughlin, Martina B. O'Keeffe, Aurélien V. Le Gouic, Philip J. Allsopp, Emeir M. McSorley, Shaun Sharkey, Jason Whooley, Brian McGovern, Finbarr P.M. O'Harte, Richard J. FitzGerald

Research output: Contribution to journalArticlepeer-review

Abstract

Twenty-two novel dipeptidyl peptidase-IV (DPP-IV) inhibitory peptides (with IC50 values <200 µM) and fifteen novel insulinotropic peptides were identified in a boarfish protein hydrolysate generated at semi-pilot scale using Alcalase 2.4L and Flavourzyme 500L. This was achieved by bioassay-driven semi-preparative reverse phase-high performance liquid chromatography fractionation, liquid chromatography-mass spectrometry and confirmatory studies with synthetic peptides. The most potent DPP-IV inhibitory peptide (IPVDM) had a DPP-IV half maximal inhibitory concentration (IC50) value of 21.72 ± 1.08 µM in a conventional in vitro and 44.26 ± 0.65 µM in an in situ cell-based (Caco-2) DPP-IV inhibition assay. Furthermore, this peptide stimulated potent insulin secretory activity (1.6-fold increase compared to control) from pancreatic BRIN-BD11 cells grown in culture. The tripeptide IPV exhibited potent DPP-IV inhibitory activity (IC50: 5.61 ± 0.20 µM) comparable to that reported for the known DPP-IV inhibitor IPI (IC50: 3.20 µM). Boarfish proteins contain peptide sequences with potential to play a role in glycaemic management in vivo.

Original languageEnglish
Article number108989
Pages (from-to)108989
JournalFood Research International
Volume131
DOIs
Publication statusPublished - May 2020

Keywords

  • Bioactive peptide
  • Boarfish
  • Dipeptidyl peptidase-IV
  • Insulinotropic
  • Type 2 diabetes

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