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Effect of pore structure on protein adsorption mechanism on ion exchange media: A preliminary study using low field nuclear magnetic resonance
Chen, Chao1,2; Zhao, Dawei1; Su, Zhiguo1; Luo, Jian1; Ma, Guanghui1; Zhang, Songping1; Li, Xiunan1
2021-02-22
Source PublicationJOURNAL OF CHROMATOGRAPHY A
ISSN0021-9673
Volume1639Pages:7
AbstractThe adsorption process of bovine serum albumin (BSA), ovalbumin (OVA) and human immunoglobulin G (IgG) on agarose ion-exchange media Q Sepharose FF and two dextran-grafted agarose media including Q Sepharose XL and Capto Q were studied using low field nuclear magnetic resonance (NMR). The T-2 relaxation time was found directly proportional to the pore size and diminished after protein adsorbed, therefore, a theoretical model describing the relationship between protein binding amount and T-2 relaxation signals was established. The model parameters, a, which reflects the contact area between the adsorbed protein and media surface, and the delta, which defined as the ratio of the protein volume to the pore volume after adsorption, were found to describe the pore occupation states of proteins in media with different pore structures very well. For small proteins, such as BSA and OVA, monolayer adsorption occurred on Q Sepharose FF, which has no dextran chains. Therefore, the adsorbed protein only occupied 49.05% of the pore volume for BSA and 25.51% for OVA, and contact area of each protein on the media were also low, suggesting mostly monolayer adsorption occurred. In the contrast, their adsorption to Q Sepharose XL and Capto Q with dextran chains tended to form multilayer adsorption, thus higher contact area was obtained and the pore volumes were almost 100% occupied. For large protein, such as IgG, the adsorption to all these three media was similar and about 30% of the pore volume were occupied, probably due to the similar restriction for IgG to entering the media pore. Results of this study will help to elucidate the relationship between protein adsorption and pore size variation, which present the significance of low field NMR in understanding protein adsorption mechanism. (C) 2021 Elsevier B.V. All rights reserved.
KeywordLow field nuclear magnetic resonance Transverse relaxation time T-2 Protein adsorption process Ion exchange media
DOI10.1016/j.chroma.2021.461904
Language英语
WOS KeywordLASER-SCANNING MICROSCOPY ; SIZE DISTRIBUTIONS ; MESOPOROUS SILICA ; AGAROSE MEDIA ; TRANSPORT ; CHROMATOGRAPHY ; PARTICLES ; ADSORBENTS ; DIFFUSION ; KINETICS
Funding ProjectNational Natural Science Foundation of China[21821005] ; National Natural Science Foundation of China[21376248] ; National Natural Science Foundation of China[21506228]
WOS Research AreaBiochemistry & Molecular Biology ; Chemistry
WOS SubjectBiochemical Research Methods ; Chemistry, Analytical
Funding OrganizationNational Natural Science Foundation of China
WOS IDWOS:000687137800012
PublisherELSEVIER
Citation statistics
Document Type期刊论文
Identifierhttp://ir.ipe.ac.cn/handle/122111/49926
Collection中国科学院过程工程研究所
Corresponding AuthorZhang, Songping; Li, Xiunan
Affiliation1.Chinese Acad Sci, Inst Proc Engn, State Key Lab Biochem Engn, Beijing 100190, Peoples R China
2.Univ Chinese Acad Sci, Sch Chem Engn, Beijing 100049, Peoples R China
Recommended Citation
GB/T 7714
Chen, Chao,Zhao, Dawei,Su, Zhiguo,et al. Effect of pore structure on protein adsorption mechanism on ion exchange media: A preliminary study using low field nuclear magnetic resonance[J]. JOURNAL OF CHROMATOGRAPHY A,2021,1639:7.
APA Chen, Chao.,Zhao, Dawei.,Su, Zhiguo.,Luo, Jian.,Ma, Guanghui.,...&Li, Xiunan.(2021).Effect of pore structure on protein adsorption mechanism on ion exchange media: A preliminary study using low field nuclear magnetic resonance.JOURNAL OF CHROMATOGRAPHY A,1639,7.
MLA Chen, Chao,et al."Effect of pore structure on protein adsorption mechanism on ion exchange media: A preliminary study using low field nuclear magnetic resonance".JOURNAL OF CHROMATOGRAPHY A 1639(2021):7.
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