CAS OpenIR  > 研究所(批量导入)
Residue-level elucidation of the ligand-induced protein binding on phenyl-argarose microspheres by NMR hydrogen/deuterium exchange technique
Alternative TitleSoft Matter
Hao, Dong-Xia1,2; Sandstrom, Corine2; Huang, Yong-Dong1; Kenne, Lennart2; Janson, Jan-Christer3; Ma, Guang-Hui1; Su, Zhi-Guo1
2012
Source PublicationSOFT MATTER
ISSN1744-683X
Volume8Issue:23Pages:6248-6255
AbstractProtein-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.; 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.
KeywordHydrophobic Interaction Chromatography Egg-white Lysozyme Molten Globule State Hydrogen-exchange Cytochrome-c Conformational-changes Nanoparticle Size Density Adsorption Retention
SubtypeArticle
WOS HeadingsScience & Technology ; Physical Sciences ; Technology
DOI10.1039/c2sm25117e
URL查看原文
Indexed BySCI
Language英语
WOS KeywordHYDROPHOBIC INTERACTION CHROMATOGRAPHY ; EGG-WHITE LYSOZYME ; MOLTEN GLOBULE STATE ; HYDROGEN-EXCHANGE ; CYTOCHROME-C ; CONFORMATIONAL-CHANGES ; NANOPARTICLE SIZE ; DENSITY ; ADSORPTION ; RETENTION
WOS Research AreaChemistry ; Materials Science ; Physics ; Polymer Science
WOS SubjectChemistry, Physical ; Materials Science, Multidisciplinary ; Physics, Multidisciplinary ; Polymer Science
WOS IDWOS:000304309300009
Citation statistics
Cited Times:3[WOS]   [WOS Record]     [Related Records in WOS]
Document Type期刊论文
Version出版稿
Identifierhttp://ir.ipe.ac.cn/handle/122111/6473
Collection研究所(批量导入)
Affiliation1.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
Recommended Citation
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.
Files in This Item:
File Name/Size DocType Version Access License
Residue-level elucid(1778KB) 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
[Hao, Dong-Xia]'s Articles
[Sandstrom, Corine]'s Articles
[Huang, Yong-Dong]'s Articles
Baidu academic
Similar articles in Baidu academic
[Hao, Dong-Xia]'s Articles
[Sandstrom, Corine]'s Articles
[Huang, Yong-Dong]'s Articles
Bing Scholar
Similar articles in Bing Scholar
[Hao, Dong-Xia]'s Articles
[Sandstrom, Corine]'s Articles
[Huang, Yong-Dong]'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.