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

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.