Potential DPP IV Inhibitory Peptides from Dry-Cured Pork Loins after Hydrolysis: An In Vitro and In Silico Study

Curr Issues Mol Biol. 2021 Sep 27;43(3):1335-1349. doi: 10.3390/cimb43030095.

Abstract

Peptidyl peptidase IV (DPP-IV) is a pharmacotherapeutic target in type 2 diabetes, and inhibitors of this enzyme are an important class of drugs for the treatment of type 2 diabetes. In the present study, peptides (<7 kDa) isolated from dry-cured pork loins after pepsin and pancreatin hydrolysis were identified by mass spectrometry and tested as potential inhibitors of DPP-IV by the in silico method. Two peptides, namely WTIAVPGPPHS from myomesin (water-soluble fraction, A = 0.9091) and FKRPPL from troponin (salt-soluble fraction, A = 0.8333), were selected as the most promising inhibitors of DPP-IV. Both peptides were subjected to ADMET analysis. Fragments of these peptides showed promising drug-likeness properties as well as favorable absorption, distribution, metabolism, excretion, and toxicity functions, suggesting that they are novel leads in the development of DPP-IV inhibitors from food.

Keywords: DPP-IV; dry-cured meat; peptides; spectrometric analysis.

MeSH terms

  • Amino Acid Sequence
  • Chemical Fractionation
  • Dipeptidyl-Peptidase IV Inhibitors / chemistry*
  • Dipeptidyl-Peptidase IV Inhibitors / isolation & purification
  • Dipeptidyl-Peptidase IV Inhibitors / metabolism
  • Hydrolysis
  • Muscle Proteins / chemistry
  • Muscle Proteins / isolation & purification
  • Peptides / chemistry*
  • Peptides / isolation & purification
  • Peptides / metabolism
  • Pork Meat* / analysis
  • Protein Binding
  • Protein Interaction Mapping
  • Protein Interaction Maps
  • Spectrum Analysis
  • Structure-Activity Relationship

Substances

  • Dipeptidyl-Peptidase IV Inhibitors
  • Muscle Proteins
  • Peptides