CAS OpenIR  > 研究所(批量导入)
Microcalorimetric study of adsorption and disassembling of virus-like particles on anion exchange chromatography media
Yu, Mengran1,2,3; Zhang, Songping1,2,4; Zhang, Yan1,2; Yang, Yanli1,2,3; Ma, Guanghui1,2; Su, Zhiguo1,2,4
2015-04-03
Source PublicationJOURNAL OF CHROMATOGRAPHY A
ISSN0021-9673
Volume1388Issue:APRPages:195-206
Abstract

Chromatographic purification of virus-like particles (VLPs) is important to the development of modern vaccines. However, disassembly of the VLPs on the solid-liquid interface during chromatography process could be a serious problem. In this study, isothermal titration calorimetric (ITC) measurements, together with chromatography experiments, were performed on the adsorption and disassembling of multi-subunits hepatitis B virus surface antigen virus-like particles (HB-VLPs). Two gigaporous ion-exchange chromatography (IEC) media, DEAE-AP-280 nm and DEAE-POROS, were used. The application of gigaporous media with high ligand density led to significantly increased irreversible disassembling of HB-VLPs and consequently low antigen activity recovery during IEC process. To elucidate the thermodynamic mechanism of the effect of ligand density on the adsorption and conformational change of VLPs, a thermodynamic model was proposed. With this model, one can obtain the intrinsic molar enthalpy changes related to the binding of VLPs and the accompanying conformational change on the liquid-solid interface during its adsorption. This model assumes that, when intact HB-VLPs interact with the IEC media, the total adsorbed proteins contain two states, the intact formation and the disassembled formation; accordingly, the apparent adsorption enthalpy, Delta H-app, which can be directly measured from ITC experiments, presents the sum of three terms: (1) the intrinsic molar enthalpy change associated to the binding of intact HB-VLps s Delta H-bind(intact), 1 (2) the intrinsic molar enthalpy change associated to the binding of HB-VLPs disassembled formation ( Delta H-bind(dis)), and (3) the enthalpy change accompanying the disassembling of HB-VLPs (Delta H-conf(dis)). The intrinsic binding of intact HB-VLPs and the disassembled HB-VLPs to both kinds of gigaporous media (each of which has three different ligand densities), were all observed to be entropically driven as indicated by positive values of Delta H-bind(intact) and Delta H-bind(dis) while the nagative Delta H-conf(dis) values suggested a spontenous enthalpy-driven process for the forming of HB-VLPs disassembled formation at all conditions studied. As ligand density increases, Delta H-conf(dis) became more negative, which was in agreement with the findings from chromatography experiments, that higher ligand density leads to more serious disassembling of HB-VLPs. Results from thermodynamic studies provided us insight understanding on the mechanism of adsorption and conformational change of VLPs, as well as the effect of ligand densities on the structural stability of VLPs during IEC process. (C) 2015 Elsevier B.V. All rights reserved.

KeywordIsothermal Titration Calorimetry Hepatitis b Virus Surface Antigen Virus-like Particles Gigaporous Media Ion Exchange Chromatography Conformational Change
SubtypeArticle
Subject AreaBiochemistry & Molecular Biology ; Chemistry
WOS HeadingsScience & Technology ; Life Sciences & Biomedicine ; Physical Sciences
DOI10.1016/j.chroma.2015.02.048
Indexed BySCI
Language英语
WOS KeywordIsothermal Titration Calorimetry ; Bovine Serum-albumin ; b Surface-antigen ; Ion-exchange ; Pegylated Lysozyme ; Protein Adsorption ; Stability ; Resin ; Temperature ; Supports
Funding ProjectNational Natural Science Foundation of China [21336010] ; National High Technology Research and Development Program of China (863 Program) [2012AA02A406, 2014AA021005]
WOS Research AreaBiochemistry & Molecular Biology ; Chemistry
WOS SubjectBiochemical Research Methods ; Chemistry, Analytical
WOS IDWOS:000351792400023
Citation statistics
Cited Times:11[WOS]   [WOS Record]     [Related Records in WOS]
Document Type期刊论文
Identifierhttp://ir.ipe.ac.cn/handle/122111/13784
Collection研究所(批量导入)
Corresponding AuthorZhang, Songping
Affiliation1.Chinese Acad Sci, Inst Proc Engn, Natl Key Lab Biochem Engn, Beijing 100190, Peoples R China
2.PLA Key Lab Biopharmaceut Proc & Formulat Engn, Beijing 100190, Peoples R China
3.Univ Chinese Acad Sci, Beijing 100049, Peoples R China
4.Collaborat Innovat Ctr Chem Sci & Engn Tianjin, Tianjin 300072, Peoples R China
Recommended Citation
GB/T 7714
Yu, Mengran,Zhang, Songping,Zhang, Yan,et al. Microcalorimetric study of adsorption and disassembling of virus-like particles on anion exchange chromatography media[J]. JOURNAL OF CHROMATOGRAPHY A,2015,1388(APR):195-206.
APA Yu, Mengran,Zhang, Songping,Zhang, Yan,Yang, Yanli,Ma, Guanghui,&Su, Zhiguo.(2015).Microcalorimetric study of adsorption and disassembling of virus-like particles on anion exchange chromatography media.JOURNAL OF CHROMATOGRAPHY A,1388(APR),195-206.
MLA Yu, Mengran,et al."Microcalorimetric study of adsorption and disassembling of virus-like particles on anion exchange chromatography media".JOURNAL OF CHROMATOGRAPHY A 1388.APR(2015):195-206.
Files in This Item:
File Name/Size DocType Version Access License
Microcalorimetric st(2070KB)期刊论文出版稿限制开放CC BY-NC-SAApplication Full Text
Related Services
Recommend this item
Bookmark
Usage statistics
Export to Endnote
Google Scholar
Similar articles in Google Scholar
[Yu, Mengran]'s Articles
[Zhang, Songping]'s Articles
[Zhang, Yan]'s Articles
Baidu academic
Similar articles in Baidu academic
[Yu, Mengran]'s Articles
[Zhang, Songping]'s Articles
[Zhang, Yan]'s Articles
Bing Scholar
Similar articles in Bing Scholar
[Yu, Mengran]'s Articles
[Zhang, Songping]'s Articles
[Zhang, Yan]'s Articles
Terms of Use
No data!
Social Bookmark/Share
All comments (0)
No comment.
 

Items in the repository are protected by copyright, with all rights reserved, unless otherwise indicated.