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Adsorption of virus-like particles on ion exchange surface: Conformational changes at different pH detected by dual polarization interferometry
Yang, Yanli1,2; Yu, Mengran1,2; Zhang, Songping1; Ma, Guanghui1; Su, Zhiguo1
2015-08-21
Source PublicationJOURNAL OF CHROMATOGRAPHY A
ISSN0021-9673
Volume1408Issue:AUGPages:161-168
AbstractDisassembling of virus-like particles (VLPs) like hepatitis B virus surface antigen (HB-VLPs) during chromatographic process has been identified as a major cause of loss of antigen activity. In this study, dual polarization interferometry (DPI) measurement, together with chromatography experiments, were performed to study the adsorption and conformational change of HB-VLPs on ion exchange surface at three different pHs. Changes in pH values of buffer solution showed only minimal effect on the HB-VLPs assembly and antigen activity, while significantly different degree of HB-VLPs disassembling was observed after ion exchange chromatography (IEC) at different pHs, indicating the conformational change of HB-VLPs caused mainly by its interactions with the adsorbent surface. By creating an ion exchange surface on chip surface, the conformational changes of HB-VLPs during adsorption to the surface were monitored in real time by DPI for the first time. As pH increased from 7.0 to 9.0, strong electrostatic interactions between oppositely charged HB-VLPs and the ion exchange surface make the HB-VLPs spread thinly or even adsorbed in disassembled formation on the surface as revealed by significant decrease in thickness of the adsorbed layer measured by DPI. Such findings were consistent with the results of IEC experiments operated at different pHs, that more disassembled HB-VLPs were detected in the eluted proteins at pH 9.0. At low pH like pH 5.0, however, possible hi-layer adsorption was involved as evidenced by an adsorbed layer thickness higher than average diameter of the HB-VLPs. The "lateral" protein protein interactions might be unfavorable and would make additional contribution to the disassembling of HB-VLPs besides the primary mechanism related to the protein surface interactions; therefore, the lowest antigen activity was observed after IEC at pH 5.0. Such real-time information on conformational change of VLPs is helpful for better understanding the real mechanism for the disassembling of VLPs on the solid liquid interface. (C) 2015 Elsevier B.V. All rights reserved.
KeywordVirus-like Particles Dual Polarization Interferometry Conformational Change Ion Exchange Chromatography
SubtypeArticle
WOS HeadingsScience & Technology ; Life Sciences & Biomedicine ; Physical Sciences
DOI10.1016/j.chroma.2015.07.019
Indexed BySCI
Language英语
WOS KeywordCHINESE-HAMSTER OVARY ; HANSENULA-POLYMORPHA ; CHROMATOGRAPHIC SUPPORTS ; VACCINE DEVELOPMENT ; PROTEIN ADSORPTION ; LIGAND DENSITY ; ANTIGEN ; PURIFICATION ; STABILITY ; BINDING
WOS Research AreaBiochemistry & Molecular Biology ; Chemistry
WOS SubjectBiochemical Research Methods ; Chemistry, Analytical
WOS IDWOS:000359327100020
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Cited Times:7[WOS]   [WOS Record]     [Related Records in WOS]
Document Type期刊论文
Identifierhttp://ir.ipe.ac.cn/handle/122111/19434
Collection生化工程国家重点实验室
Affiliation1.Chinese Acad Sci, Inst Proc Engn, Natl Key Lab Biochem Engn, Beijing 100190, Peoples R China
2.Univ Chinese Acad Sci, Beijing 100049, Peoples R China
Recommended Citation
GB/T 7714
Yang, Yanli,Yu, Mengran,Zhang, Songping,et al. Adsorption of virus-like particles on ion exchange surface: Conformational changes at different pH detected by dual polarization interferometry[J]. JOURNAL OF CHROMATOGRAPHY A,2015,1408(AUG):161-168.
APA Yang, Yanli,Yu, Mengran,Zhang, Songping,Ma, Guanghui,&Su, Zhiguo.(2015).Adsorption of virus-like particles on ion exchange surface: Conformational changes at different pH detected by dual polarization interferometry.JOURNAL OF CHROMATOGRAPHY A,1408(AUG),161-168.
MLA Yang, Yanli,et al."Adsorption of virus-like particles on ion exchange surface: Conformational changes at different pH detected by dual polarization interferometry".JOURNAL OF CHROMATOGRAPHY A 1408.AUG(2015):161-168.
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