Protein O-Glycosylation Research Based on a Glycoform Library Strategy
Covalent attachment of glycans to the side chains of protein amino acids can form glycosylation.Glycosylation,in many cases,significantly increases the diversity of protein structure,properties,and functions.Specific glycosylation patterns can confer specific effects on proteins and enzymes,while aberrant glycosylation patterns may lead to diseases.Therefore,a comprehensive understanding of the role of protein glycosylation is of great significance,both for basic and applied research.However,progress in this area has been exceptionally slow due to the difficulty in obtaining suitable samples for study.In recent years,researchers have gradually begun to explore the use of a library-based strategy to change this situation.This strategy involves the synthetic preparation and characterization of a series of homogeneously glycosylated protein isoforms(glycoforms)with high purity and systematic variations in structures.Through the following comparative analysis,the effects and functioning mechanisms of protein glycosylation can be relatively quickly and accurately obtained.This,in turn,enhances the application of glycosylation in improving the performance of proteins and enzymes.This review aims to summarize,outline,and briefly discuss the progress in the O-glycosylation research direction.It presents research methods and achievements of a few existing examples in chronological order,with the aim of helping researchers gain a clearer understanding of the current development and shortcomings of this strategy.This review is expected to assist researchers in better utilizing this strategy for protein glycosylation research and applications,ultimately improving the depth and breadth of this research.
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