Sialic acid linkage-specific permethylation for improved profiling of protein glycosylation by MALDI-TOF MS.

ABSTRACT: Protein glycosylation mediates a wide range of cellular processes, affecting development and disease in mammals. Deciphering the "glycocodes" requires rapid, sensitive and in-depth characterization of diverse glycan structures derived from biological samples. In this study, we described a two-step derivatization strategy termed linkage-specific sialic acid permethylation (SSAP) consisting of dimethylamination and permethylation for the improved profiling of glycosylation by matrix-assisted laser desorption/ionization (MALDI) time-of-fight (TOF) mass spectrometry (MS). High linkage-specificity (∼99%) of SSAP to both the two most common forms of sialic acid, N-acetylneuraminic acid (Neu5Ac) and N-glycolylneuraminic acid (Neu5Gc), permitted direct discrimination of α2,3- and α2,6-linked siali

SUBMITTER: Jiang K 

PROVIDER: S-EPMC5953179 | biostudies-literature | 2017 Aug

REPOSITORIES: biostudies-literature