Differential glycosylation does not modulate the conformational heterogeneity of a humanised IgGk NIST monoclonal antibody

被引：0
|
作者：
Liu, Fanny C. [1 ]
Lee, Jusung [1 ]
Pedrete, Thais [1 ]
Panczyk, Erin M. [2 ]
Pengelley, Stuart [3 ]
Bleiholder, Christian [1 ,4 ]
机构：
[1] Florida State Univ, Dept Chem & Biochem, 102 Vars Way, Tallahassee, FL 32306 USA
[2] Bruker Daltonics Inc, 40 Manning Rd, Billerica, MA 01821 USA
[3] Bruker Dalton GmbH&Co, Fahrenheitstr 4, D-28359 Bremen, Germany
[4] Florida State Univ, Inst Mol Biophys, 91 Chieftan Way, Tallahassee, FL 32306 USA
来源：
CHEMICAL COMMUNICATIONS | 2024年 / 60卷 / 77期
基金：
美国国家卫生研究院; 美国国家科学基金会;
关键词：
MOBILITY-MASS-SPECTROMETRY; ION-MOBILITY; STABILITY; DYNAMICS;
D O I：
10.1039/d4cc02125h
中图分类号：
O6 [化学];
学科分类号：
0703 ;
摘要：
Investigating the structural heterogeneity of monoclonal antibodies is crucial to achieving optimal therapeutic outcomes. We show that tandem-trapped ion mobility spectrometry enables collision-induced unfolding measurements of subpopulations of a humanised IgGk NIST monoclonal antibody (NISTmAb). Our results indicate that differential glycosylation of NISTmAb does not modulate its conformational heterogeneity. Tandem ion mobility spectrometry reveals that glycosylation does not alter the conformational heterogeneity of a monoclonal antibody.
引用
收藏
页码：10740 / 10743
页数：4
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