Sialylation-induced stabilization of dynamic glycoprotein conformations unveiled by time-aligned parallel unfolding and glycan release mass spectrometry-Reference-Cited by-同舟云学术

Sialylation-induced stabilization of dynamic glycoprotein conformations unveiled by time-aligned parallel unfolding and glycan release mass spectrometry

Published:2024 Issue:35 Volume:15 Page:14431-14439
ISSN:2041-6520
Container-title:Chemical Science
language:en
Short-container-title:Chem. Sci.

Author:

Jia Yifei¹,Liu Yichang²^ORCID,Wang Yamei¹,Li Jinyu³^ORCID,Li Gongyu¹⁴^ORCID

Affiliation:

1. Tianjin Key Laboratory of Biosensing and Molecular Recognition, Research Center for Analytical Science, Frontiers Science Center for New Organic Matter, College of Chemistry, Nankai University, Tianjin 300071, China

2. School of Pharmacy, Nantong University, Nantong 226001, Jiangsu, China

3. College of Chemistry, Fuzhou University, Fuzhou 350108, Fujian, China

4. Haihe Laboratory of Sustainable Chemical Transformations, Tianjin 300192, China

Abstract

A glycoform-resolved unfolding ion mobility-mass spectrometry approach reveals how sialylation patterns modulate glycoprotein conformational stability and dynamics, providing insights into the relationship between sialylation and protein structure.

Funder

National Natural Science Foundation of China

Fundamental Research Funds for the Central Universities

Nankai University

Publisher

Royal Society of Chemistry (RSC)

Link

http://pubs.rsc.org/en/content/articlepdf/2024/SC/D4SC03672G

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4. The Mechanistic Impact of N-Glycosylation on Stability, Pharmacokinetics, and Immunogenicity of Therapeutic Proteins

5. Native Ion Mobility–Mass Spectrometry-Enabled Fast Structural Interrogation of Labile Protein Surface Modifications at the Intact Protein Level