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| Residue-level elucidation of the ligand-induced protein binding on phenyl-argarose microspheres by NMR hydrogen/deuterium exchange technique | |
| Alternative Title | Soft Matter |
| Hao, Dong-Xia1,2; Sandstrom, Corine2; Huang, Yong-Dong1; Kenne, Lennart2; Janson, Jan-Christer3; Ma, Guang-Hui1; Su, Zhi-Guo1 | |
| 2012 | |
| Source Publication | SOFT MATTER
 |
| ISSN | 1744-683X |
| Volume | 8Issue:23Pages:6248-6255 |
| Abstract | 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.; 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. |
| Keyword | Hydrophobic Interaction Chromatography Egg-white Lysozyme Molten Globule State Hydrogen-exchange Cytochrome-c Conformational-changes Nanoparticle Size Density Adsorption Retention |
| Subtype | Article |
| WOS Headings | Science & Technology ; Physical Sciences ; Technology |
| DOI | 10.1039/c2sm25117e |
| URL | 查看原文 |
| Indexed By | SCI |
| Language | 英语 |
| WOS Keyword | HYDROPHOBIC INTERACTION CHROMATOGRAPHY ; EGG-WHITE LYSOZYME ; MOLTEN GLOBULE STATE ; HYDROGEN-EXCHANGE ; CYTOCHROME-C ; CONFORMATIONAL-CHANGES ; NANOPARTICLE SIZE ; DENSITY ; ADSORPTION ; RETENTION |
| WOS Research Area | Chemistry ; Materials Science ; Physics ; Polymer Science |
| WOS Subject | Chemistry, Physical ; Materials Science, Multidisciplinary ; Physics, Multidisciplinary ; Polymer Science |
| WOS ID | WOS:000304309300009 |
| Citation statistics | |
| Document Type | 期刊论文 |
| Version | 出版稿 |
| Identifier | http://ir.ipe.ac.cn/handle/122111/6473 |
| Collection | 研究所（批量导入） |
| Affiliation | 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 |
| 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. |
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| Residue-level elucid（1778KB） | 限制开放 | CC BY-NC-SA | Application Full Text | |||
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