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	Residue-level elucidation of the ligand-induced protein binding on phenyl-argarose microspheres by NMR hydrogen/deuterium exchange technique
	Hao, Dong-Xia1,2; Sandstrom, Corine2; Huang, Yong-Dong1; Kenne, Lennart2; Janson, Jan-Christer3; Ma, Guang-Hui1; Su, Zhi-Guo1
刊名	SOFT MATTER
	2012
卷号	8期号:23页码:6248-6255
关键词	hydrophobic interaction chromatography egg-white lysozyme molten globule state hydrogen-exchange cytochrome-c conformational-changes nanoparticle size density adsorption retention
ISSN号	1744-683X
其他题名	Soft Matter
中文摘要	Protein-ligand interactions on liquid-solid interfaces governed the design of functional biomaterials. However, accurate residue details of ligand induced protein binding and unfolding on an interface were still unknown by the current ensemble of protein structure characterizations. Here, a hydrogen/deuterium (H/D) approach coupled with analysis of NMR TOCSY spectra and the solvent accessible surface area (SASA) was designed to enable residue level understanding of lysozyme adsorbed at a phenyl-ligand modified surface. Results showed that the binding sites and unfolding of lysozyme molecules on phenyl-agarose microspheres demonstrated significant ligand-density dependence and protein-coverage dependence. Either increasing ligand density or decreasing adsorption coverage would lead to more binding sites and unfolding of the protein molecules. With the multipoint adsorption strengthening, the protein molecule changed from lying end-on to side-on. Finally, Molecular Dock simulation was utilized to evaluate the NMR determined binding sites based on energy ranking of the binding. It confirmed that this NMR approach represents a reliable route to in silico abundant residue-level structural information during protein interaction with biomaterials.
英文摘要	Protein-ligand interactions on liquid-solid interfaces governed the design of functional biomaterials. However, accurate residue details of ligand induced protein binding and unfolding on an interface were still unknown by the current ensemble of protein structure characterizations. Here, a hydrogen/deuterium (H/D) approach coupled with analysis of NMR TOCSY spectra and the solvent accessible surface area (SASA) was designed to enable residue level understanding of lysozyme adsorbed at a phenyl-ligand modified surface. Results showed that the binding sites and unfolding of lysozyme molecules on phenyl-agarose microspheres demonstrated significant ligand-density dependence and protein-coverage dependence. Either increasing ligand density or decreasing adsorption coverage would lead to more binding sites and unfolding of the protein molecules. With the multipoint adsorption strengthening, the protein molecule changed from lying end-on to side-on. Finally, Molecular Dock simulation was utilized to evaluate the NMR determined binding sites based on energy ranking of the binding. It confirmed that this NMR approach represents a reliable route to in silico abundant residue-level structural information during protein interaction with biomaterials.
WOS标题词	Science & Technology ; Physical Sciences ; Technology
类目[WOS]	Chemistry, Physical ; Materials Science, Multidisciplinary ; Physics, Multidisciplinary ; Polymer Science
研究领域[WOS]	Chemistry ; Materials Science ; Physics ; Polymer Science
关键词[WOS]	HYDROPHOBIC INTERACTION CHROMATOGRAPHY ; EGG-WHITE LYSOZYME ; MOLTEN GLOBULE STATE ; HYDROGEN-EXCHANGE ; CYTOCHROME-C ; CONFORMATIONAL-CHANGES ; NANOPARTICLE SIZE ; DENSITY ; ADSORPTION ; RETENTION
收录类别	SCI
原文出处	://WOS:000304309300009
语种	英语
WOS记录号	WOS:000304309300009
公开日期	2013-11-28
内容类型	期刊论文
版本	出版稿
源URL	[http://ir.ipe.ac.cn/handle/122111/6473]
专题	过程工程研究所_研究所（批量导入）
作者单位	1.Chinese Acad Sci, Inst Proc Engn, Natl Key Lab Biochem Engn, Beijing 100190, Peoples R China 2.Swedish Univ Agr Sci, Dept Chem, SE-75007 Uppsala, Sweden 3.Uppsala Univ, Dept Phys & Analyt Chem, SE-75123 Uppsala, Sweden
推荐引用方式 GB/T 7714	Hao, Dong-Xia,Sandstrom, Corine,Huang, Yong-Dong,et al. Residue-level elucidation of the ligand-induced protein binding on phenyl-argarose microspheres by NMR hydrogen/deuterium exchange technique[J]. SOFT MATTER,2012,8(23):6248-6255.
APA	Hao, Dong-Xia.,Sandstrom, Corine.,Huang, Yong-Dong.,Kenne, Lennart.,Janson, Jan-Christer.,...&Su, Zhi-Guo.(2012).Residue-level elucidation of the ligand-induced protein binding on phenyl-argarose microspheres by NMR hydrogen/deuterium exchange technique.SOFT MATTER,8(23),6248-6255.
MLA	Hao, Dong-Xia,et al."Residue-level elucidation of the ligand-induced protein binding on phenyl-argarose microspheres by NMR hydrogen/deuterium exchange technique".SOFT MATTER 8.23(2012):6248-6255.

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