Proteomic analysis of sweet algerian apricot kernels (Prunus armeniaca L.) by combinatorial peptide ligand libraries and LC-MS/MS

Food Chem. 2018 Jan 15:239:935-945. doi: 10.1016/j.foodchem.2017.07.054. Epub 2017 Jul 12.

Abstract

An investigation on the proteome of the sweet kernel of apricot, based on equalisation with combinatorial peptide ligand libraries (CPLLs), SDS-PAGE, nLC-ESI-MS/MS, and database search, permitted identifying 175 proteins. Gene ontology analysis indicated that their main molecular functions are in nucleotide binding (20.9%), hydrolase activities (10.6%), kinase activities (7%), and catalytic activity (5.6%). A protein-protein association network analysis using STRING software permitted to build an interactomic map of all detected proteins, characterised by 34 interactions. In order to forecast the potential health benefits deriving from the consumption of these proteins, the two most abundant, i.e. Prunin 1 and 2, were enzymatically digested in silico predicting 10 and 14 peptides, respectively. Searching their sequences in the database BIOPEP, it was possible to suggest a variety of bioactivities, including dipeptidyl peptidase-IV (DPP-IV) and angiotensin converting enzyme I (ACE) inhibition, glucose uptake stimulation and antioxidant properties.

Keywords: Apricot; Combinatorial peptide ligand libraries (CPLL); GO analysis; LC–MS/MS; Proteomics; Prunin.

MeSH terms

  • Peptide Library
  • Peptides
  • Proteomics
  • Prunus armeniaca*
  • Tandem Mass Spectrometry

Substances

  • Peptide Library
  • Peptides