Mass spectrometric evidence of malonaldehyde and 4-hydroxynonenal adductions to radical-scavenging soy peptides

Jing Zhao, Jing Chen, Haining Zhu, Youling L. Xiong

Research output: Contribution to journalArticlepeer-review

48 Scopus citations

Abstract

Antioxidative peptides in food systems are potential targets of lipid oxidation-generated reactive aldehydes, such as malonaldehyde (MDA) and 4-hydroxynonenal (HNE). In this study, covalent modifications on radical-scavenging peptides prepared from soy protein hydrolysate by MDA and HNE were characterized by liquid chromatography-electrospray ionization-mass spectrometry (LC-ESI-MS/MS). MS/MS analyses detected the formation of Schiff base type adducts of MDA on the side-chain groups of lysine, histidine, arginine, glutamine, and asparagine residues as well as the N-termini of peptides. MDA also formed a fluorescent product with lysine residues. HNE adducted on lysine residues through Schiff base formation and on histidine, arginine, glutamine, and asparagine residues mainly through Michael addition. Despite the extensive MDA modification, peptide cross-linking by this potential mechanism was undetectable.

Original languageEnglish (US)
Pages (from-to)9727-9736
Number of pages10
JournalJournal of agricultural and food chemistry
Volume60
Issue number38
DOIs
StatePublished - Sep 26 2012
Externally publishedYes

Keywords

  • 4-hydroxynonenal (HNE)
  • malonaldehyde (MDA)
  • mass spectrometry
  • peptides
  • radical-scavenging activity

ASJC Scopus subject areas

  • Chemistry(all)
  • Agricultural and Biological Sciences(all)

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