中国科学院机构知识库网格
Chinese Academy of Sciences Institutional Repositories Grid
Investigation of the effects of surface chemistry on adsorption of albumin by surface-enhanced FTIR spectroscopy

文献类型:期刊论文

作者Cao FJ ; Wang LX ; Jiang XU ; Guo LP
刊名rsc advances
出版日期2013
卷号3期号:38页码:17214-17221
ISSN号2046-2069
关键词HUMAN SERUM-ALBUMIN INFRARED-ABSORPTION SPECTROSCOPY INDUCED CONFORMATIONAL-CHANGES SELF-ASSEMBLED MONOLAYERS PROTEIN ADSORPTION QUANTUM DOTS BIOFILM FORMATION BINDING-SITES GOLD-SURFACE MEMBRANE
通讯作者jiang xu
中文摘要zwitterionic materials have recently attracted extensive attention as antifouling materials due to their stability regardless of the temperature. here we study the adsorption of one plasma protein, human serum albumin (hsa), on the zwitterionic d-penicillamine-modified gold surface by surface-enhanced infrared absorption (seira) spectroscopy. in comparison with the adsorption of hsa on a cysteamine (positive charge) and mercaptopropionic acid (negative charge)-modified gold surface, the amount of adsorbed hsa on the zwitterionic surface was less, but the native structure of the adsorbed hsa was retained, which revealed that the zwitterionic surface was resistant to the protein adsorption. the kinetics study showed that the adsorption of hsa on the three surfaces happened in one of two ways: reversible adsorption or irreversible adsorption resulting from protein unfolding. however, the time constants involved were dramatically larger when hsa was adsorbed on the zwitterionic surface, which further proved its antifouling property. the mechanism was revealed by monitoring the water adsorption. it was found that strongly hydrogen-bonded water played an important role in the protein resistance of the zwitterionic d-penicillamine-modified gold surface. in addition, competitive binding experiments with site markers revealed that hsa was adsorbed on the zwitterionic surface through domain iia and iiia and on the carboxylic acid-terminated surfaces through domain iia.
收录类别SCI收录期刊论文
语种英语
WOS记录号WOS:000325272100046
公开日期2014-04-16
源URL[http://ir.ciac.jl.cn/handle/322003/50181]  
专题长春应用化学研究所_长春应用化学研究所知识产出_期刊论文
推荐引用方式
GB/T 7714
Cao FJ,Wang LX,Jiang XU,et al. Investigation of the effects of surface chemistry on adsorption of albumin by surface-enhanced FTIR spectroscopy[J]. rsc advances,2013,3(38):17214-17221.
APA Cao FJ,Wang LX,Jiang XU,&Guo LP.(2013).Investigation of the effects of surface chemistry on adsorption of albumin by surface-enhanced FTIR spectroscopy.rsc advances,3(38),17214-17221.
MLA Cao FJ,et al."Investigation of the effects of surface chemistry on adsorption of albumin by surface-enhanced FTIR spectroscopy".rsc advances 3.38(2013):17214-17221.

入库方式: OAI收割

来源:长春应用化学研究所

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