Probing the conformational changes of ovalbumin after glycation using HDX-MS

Food Chem. 2015 Jan 1:166:62-67. doi: 10.1016/j.foodchem.2014.05.155. Epub 2014 Jun 7.

Abstract

The conformational changes of the glycated ovalbumin were studied by hydrogen/deuterium exchange coupled with high resolution mass spectrometry technique (HDX-MS). After incubation with glucose at 50 °C for 6 h, 9 glycated peptides were detected and the corresponding glycation sites were identified. The glycation extent of each peptide was relatively high, almost over 0.5 in all peptides. A detailed peptide mapping revealed that most of the peptides, including the glycated and non-glycated were protected. The glycation sites not only influence the local region but also the distant area. The enhanced hydrogen protection after glycation suggests that the protein adopts a more stable conformation.

Keywords: Conformation; Glycation; Hydrogen/deuterium exchange; Mass spectrometry; Ovalbumin.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Deuterium / chemistry*
  • Glycosylation
  • Hydrogen / chemistry
  • Mass Spectrometry / methods*
  • Ovalbumin / chemistry*
  • Peptide Mapping
  • Peptides / chemistry

Substances

  • Peptides
  • Hydrogen
  • Ovalbumin
  • Deuterium