Hydrophilic interaction liquid chromatography in the separation of glycopeptides and their isomers.

ABSTRACT: The analysis of intact glycopeptides is a challenge because of the structural variety of the complex conjugates. In this work, we used separation involving hydrophilic interaction liquid chromatography using a superficially porous particle HALO® penta-HILIC column with tandem mass spectrometric detection for the analysis of N-glycopeptides of hemopexin. We tested the effect of the mobile phase composition on retention and separation of the glycopeptides. The results indicated that the retention of the glycopeptides was the combination of partitioning and adsorption processes. Under the optimized conditions, our HILIC method showed the ability to efficiently separate the glycoforms of the same peptide backbone including separation of the isobaric glycoforms. We achieved efficient separation

SUBMITTER: Kozlik P 

PROVIDER: S-EPMC6041177 | biostudies-literature | 2018 Aug

REPOSITORIES: biostudies-literature