``Zoom-in''-a targeted database search for identification of glycation modifications analyzed by untargeted tandem mass spectrometry

Title``Zoom-in''-a targeted database search for identification of glycation modifications analyzed by untargeted tandem mass spectrometry
Publication TypeJournal Article
Year of Publication2012
AuthorsBhonsle, HS, Korwar, AM, Kesavan, SK, Bhosale, SD, Bansode, SB, Kulkarni, MJ
JournalEuropean Journal of Mass Spectrometry
Volume18
Issue6
Pagination475-481
Date PublishedJAN
Type of ArticleArticle
ISSN1469-0667
Keywordsadvanced glycation end products (AGEs), data independent acquisition, Diabetes, post-translational modifications
Abstract

Post-translational modifications (PTMs) are very important to biological function, however their identification and characterization is technically challenging. In this study, we have identified glycation modifications by nano LC-MSE, a data independent acquisition work flow, followed by database search using the Protein Lynx Global Server (PLGS). PLGS search with a complete human protein database hardly identified glycation modifications in a glycated human serum albumin (HSA), which was detected to be glycated by western blotting with advanced glycation end products (AGE) antibody and fluorescence spectroscopy. To overcome this difficulty, ``Zoom-In'' approach, a targeted database search was used to identify glycation modifications in a glycated HSA, which were further manually validated. This approach was useful for identification of glycation modifications from untargeted tandem mass spectrometry workflow such as MSE, but may require the development of a new algorithm or an upgrade of the existing software.

DOI10.1255/ejms.1203
Type of Journal (Indian or Foreign)

Foreign

Impact Factor (IF)

1.259

Divison category: 
Biochemical Sciences