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Microscopic insight into role of protein flexibility during ion exchange chromatography by nuclear magnetic resonance and quartz crystal microbalance approaches
Hao, Dongxia; Ge, Jia; Huang, Yongdong; Zhao, Lan; Ma, Guanghui; Su, Zhiguo; Ma, GH
2016-03-18
发表期刊JOURNAL OF CHROMATOGRAPHY A
ISSN0021-9673
卷号1438期号:MAR页码:65-75
摘要Driven by the prevalent use of ion exchange chromatography (IEC) for polishing therapeutic proteins, many rules have been formulated to summarize the different dependencies between chromatographic data and various operational parameters of interest based on statically determined interactions. However, the effects of the unfolding of protein structures and conformational stability are not as well understood. This study focuses on how the flexibility of proteins perturbs retention behavior at the molecular scale using microscopic characterization approaches, including hydrogen-deuterium (H/D) exchange detected by NMR and a quartz crystal microbalance (QCM). The results showed that a series of chromatographic retention parameters depended significantly on the adiabatic compressibility and structural flexibility of the protein. That is, softer proteins with higher flexibility tended to have longer retention times and stronger affinities on SP Sepharose adsorbents. Tracing the underlying molecular mechanism using NMR and QCM indicated that an easily unfolded flexible protein with a more compact adsorption layer might contribute to the longer retention time on adsorbents. The use of NMR and QCM provided a previously unreported approach for elucidating the effect of protein structural flexibility on binding in IEC systems. (C) 2016 Published by Elsevier B.V.
关键词Iec Protein Structural Flexibility Retention Time Nmr Qcm
文章类型Article
WOS标题词Science & Technology ; Life Sciences & Biomedicine ; Physical Sciences
DOI10.1016/j.chroma.2016.02.010
URL查看原文
收录类别SCI
语种英语
关键词[WOS]HYDROPHOBIC INTERACTION CHROMATOGRAPHY ; GLYCOSYLATED MONOCLONAL-ANTIBODY ; GLOBULAR-PROTEINS ; CHARGE-DISTRIBUTION ; ADSORPTION ; RETENTION ; BEHAVIOR ; BINDING ; SURFACE ; COMPRESSIBILITY
WOS研究方向Biochemistry & Molecular Biology ; Chemistry
WOS类目Biochemical Research Methods ; Chemistry, Analytical
项目资助者National Natural Science Foundation of China(21336010 ; National Key Technology R&D Program of the Ministry of Science and Technology(2013BAB01B03) ; 21106161 ; 20820102036)
WOS记录号WOS:000371941500008
引用统计
文献类型期刊论文
条目标识符http://ir.ipe.ac.cn/handle/122111/20646
专题研究所(批量导入)
通讯作者Ma, GH
作者单位Chinese Acad Sci, Inst Proc Engn, Natl Key Lab Biochem Engn, POB 353, Beijing 100190, Peoples R China
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Hao, Dongxia,Ge, Jia,Huang, Yongdong,et al. Microscopic insight into role of protein flexibility during ion exchange chromatography by nuclear magnetic resonance and quartz crystal microbalance approaches[J]. JOURNAL OF CHROMATOGRAPHY A,2016,1438(MAR):65-75.
APA Hao, Dongxia.,Ge, Jia.,Huang, Yongdong.,Zhao, Lan.,Ma, Guanghui.,...&Ma, GH.(2016).Microscopic insight into role of protein flexibility during ion exchange chromatography by nuclear magnetic resonance and quartz crystal microbalance approaches.JOURNAL OF CHROMATOGRAPHY A,1438(MAR),65-75.
MLA Hao, Dongxia,et al."Microscopic insight into role of protein flexibility during ion exchange chromatography by nuclear magnetic resonance and quartz crystal microbalance approaches".JOURNAL OF CHROMATOGRAPHY A 1438.MAR(2016):65-75.
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