Microscopic insight into role of protein flexibility during ion exchange chromatography by nuclear magnetic resonance and quartz crystal microbalance approaches
文献类型：期刊论文
| 作者 | Hao, Dongxia; Ge, Jia; Huang, Yongdong; Zhao, Lan; Ma, Guanghui; Su, Zhiguo |
| 刊名 | JOURNAL OF CHROMATOGRAPHY A
 |
| 出版日期 | 2016-03-18 |
| 卷号 | 1438期号:MAR页码:65-75 |
| 关键词 | IEC Protein structural flexibility Retention time NMR QCM |
| ISSN号 | 0021-9673 |
| 通讯作者 | Ma, GH |
| 英文摘要 | 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. |
| WOS标题词 | Science & Technology ; Life Sciences & Biomedicine ; Physical Sciences |
| 类目[WOS] | Biochemical Research Methods ; Chemistry, Analytical |
| 研究领域[WOS] | Biochemistry & Molecular Biology ; Chemistry |
| 关键词[WOS] | HYDROPHOBIC INTERACTION CHROMATOGRAPHY ; GLYCOSYLATED MONOCLONAL-ANTIBODY ; GLOBULAR-PROTEINS ; CHARGE-DISTRIBUTION ; ADSORPTION ; RETENTION ; BEHAVIOR ; BINDING ; SURFACE ; COMPRESSIBILITY |
| 收录类别 | SCI |
| 原文出处 | ELSEVIER SCIENCE BV |
| 语种 | 英语 |
| WOS记录号 | WOS:000371941500008 |
| 源URL | [http://ir.ipe.ac.cn/handle/122111/20646]  |
| 专题 | 过程工程研究所_研究所（批量导入） |
| 作者单位 | Chinese Acad Sci, Inst Proc Engn, Natl Key Lab Biochem Engn, POB 353, Beijing 100190, Peoples R China |
| 推荐引用方式 GB/T 7714 | 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,&Su, Zhiguo.(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. |
入库方式： OAI收割
来源：过程工程研究所
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