Effect of grafted PEG chain conformation on albumin and lysozyme adsorption: A combined study using QCM-D and DPI

	Effect of grafted PEG chain conformation on albumin and lysozyme adsorption: A combined study using QCM-D and DPI
	Jin,Jing; Han,Yuanyuan; Zhang,Chang; Liu,Jingchuan; Jiang,Wei; Yin,Jinghua; Liang,Haojun
刊名	colloids and surfaces b-biointerfaces
	2015
卷号	136 页码:838-844
关键词	QUARTZ-CRYSTAL MICROBALANCE DUAL-POLARIZATION INTERFEROMETRY SELF-ASSEMBLED MONOLAYERS AIR-WATER-INTERFACE PROTEIN ADSORPTION POLYETHYLENE OXIDE POLYELECTROLYTE MULTILAYERS FIBRINOGEN ADSORPTION HYDROPHOBIC SURFACES REAL-TIME
通讯作者	jiang,w
英文摘要	in this study, elucidation of protein adsorption mechanism is performed using dual polarization interferometry (dpi) and quartz crystal microbalance with dissipation (qcm-d) to study adsorption behaviors of bovine serum albumin (bsa) and lysozyme (lyz) on poly (ethylene glycol) (peg) layers. from the analysis of dpi, peg2000 and peg5000 show tight and loose mushroom conformations, respectively. small amount of lyz could displace the interfacial water surrounding the tight mushroomed peg2000 chains by hydrogen bond attraction, leading to protein adsorption. the loose mushroomed peg5000 chains exhibit a more flexible conformation and high elastic repulsion energy that could prevent protein adsorption of all bsa and most of lyz. from the analysis of qcm, peg2000 and peg5000 show tight and extended brush conformations. the lyz adsorbed mass has critical regions of peg2000 (0.19 chain/nm(2)) and peg5000 (0.16 chain/nm(2)) graft density. when graft density of peg is higher than the critical region (brush conformations), the attraction of hydrogen bonds between peg and lyz is the dominant factor. when graft density of peg is lower than the critical region (mushroom conformations), elastic repulsion between peg and proteins is driven by the high conformation entropy of peg chains, which is the dominant force of steric repulsion in peg-protein systems. therefore, the adsorption of bsa is suppressed by the high elastic repulsion energy of peg chains, whereas the adsorption of lyz is balanced by the interactions between the repulsion of entropy elasticity and the attraction of hydrogen bonds. (c) 2015 elsevier b.v. all rights reserved.
收录类别	SCI
语种	英语
WOS记录号	WOS:000367408100102
公开日期	2016-05-31
内容类型	期刊论文
源URL	[http://ir.ciac.jl.cn/handle/322003/65179]
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	Jin,Jing,Han,Yuanyuan,Zhang,Chang,et al. Effect of grafted PEG chain conformation on albumin and lysozyme adsorption: A combined study using QCM-D and DPI[J]. colloids and surfaces b-biointerfaces,2015,136:838-844.
APA	Jin,Jing.,Han,Yuanyuan.,Zhang,Chang.,Liu,Jingchuan.,Jiang,Wei.,...&Liang,Haojun.(2015).Effect of grafted PEG chain conformation on albumin and lysozyme adsorption: A combined study using QCM-D and DPI.colloids and surfaces b-biointerfaces,136,838-844.
MLA	Jin,Jing,et al."Effect of grafted PEG chain conformation on albumin and lysozyme adsorption: A combined study using QCM-D and DPI".colloids and surfaces b-biointerfaces 136(2015):838-844.