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从天然质谱角度探讨糖蛋白结构异质性与功能的关系。

Relating glycoprotein structural heterogeneity to function - insights from native mass spectrometry.

机构信息

Department of Chemistry, Physical and Theoretical Chemistry Laboratory, University of Oxford, South Parks Road, Oxford, OX1 3QZ, UK.

出版信息

Curr Opin Struct Biol. 2019 Oct;58:241-248. doi: 10.1016/j.sbi.2019.05.019. Epub 2019 Jul 18.

Abstract

Glycosylation is the most complex and prevalent protein modification that influences attributes ranging from cellular localization and signaling to half-life and proteolysis. Glycoconjugates are fundamental for cellular function and alterations in their structure are often observed in pathological states. Most biotherapeutic proteins are glycosylated, which influences drug safety and efficacy. Therefore, the ability to characterize glycoproteins is important in all areas of biomolecular and medicinal research. Here we discuss recent advances in native mass spectrometry that have significantly improved our ability to characterize heterogeneous glycoproteins and to relate glycan structure to protein function.

摘要

糖基化是最复杂和普遍的蛋白质修饰,影响从细胞定位和信号传递到半衰期和蛋白水解的各种属性。糖缀合物是细胞功能的基础,其结构的改变在病理状态下经常观察到。大多数生物治疗蛋白都是糖基化的,这会影响药物的安全性和疗效。因此,能够对糖蛋白进行特征分析在生物分子和医学研究的所有领域都很重要。在这里,我们讨论了近年来在天然质谱方面的进展,这些进展显著提高了我们对异质糖蛋白进行特征分析的能力,并使我们能够将聚糖结构与蛋白质功能联系起来。

https://cdn.ncbi.nlm.nih.gov/pmc/blobs/530f/7104348/ce44323a35b9/EMS85670-f001.jpg

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