| Applying flexible molecular docking to simulate protein retention behavior in hydrophobic interaction chromatography |
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| 作者单位： | ZHOU Peng（College of Chemistry and Chemical Engineering, Chongqing University, Chongqing 400044, China） ;TIAN FeiFei（College of Chemistry and Chemical Engineering, Chongqing University, Chongqing 400044, China） ;LI ZhiLiang（College of Chemistry and Chemical Engineering, Chongqing University, Chongqing 400044, China;State Key Laboratory of Chemo/Biosensing and Chemometrics, Changsha 410082, China） ; |
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| 基金项目： | 国家高技术研究发展计划(863计划) |
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| 摘 要： | Interaction between proteins and stationary phase in hydrophobic interaction chromatography (HIC) is differentiated into two thermodynamic processes involving direct nonbonding/conformation interac- tion and surface hydrophobic effect of proteins, hence quantitatively giving rise to a binary linear rela- tion between HIC retention time (RT) at concentrated salting liquid and ligand-protein binding free en- ergy. Then, possible binding manners for 27 proteins of known crystal structures with hydrophobic ligands are simulated and analyzed via ICM flexible molecular docking and genetic algorithm, with re- sults greatly consistent with experimental values. By investigation, it is confirmed local hydrophobic effects of proteins and nonbinding/conformation interaction between ligand and protein both notably influence HIC chromatogram retention behaviors, mainly focusing on exposed portions on the protein surface.
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| 收稿时间： | 2006-07-05 |
| 修稿时间： | 2006-09-23 |
Applying flexible molecular docking to simulate protein retention behavior in hydrophobic interaction chromatography |
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| Zhou Peng,Tian FeiFei,Li ZhiLiang. Applying flexible molecular docking to simulate protein retention behavior in hydrophobic interaction chromatography[J]. Science in China(Chemistry), 2007, 50(5): 675-682. DOI: 10.1007/s11426-007-0044-6 |
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| Authors: | Zhou Peng Tian FeiFei Li ZhiLiang |
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| Affiliation: | 1. College of Chemistry and Chemical Engineering, Chongqing University, Chongqing 400044, China
2. College of Chemistry and Chemical Engineering, Chongqing University, Chongqing 400044, China;State Key Laboratory of Chemo/Biosensing and Chemometrics, Changsha 410082, China |
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| Abstract: | Interaction between proteins and stationary phase in hydrophobic interaction chromatography (HIC) is differentiated into two thermodynamic processes involving direct nonbonding/conformation interac- tion and surface hydrophobic effect of proteins, hence quantitatively giving rise to a binary linear rela- tion between HIC retention time (RT) at concentrated salting liquid and ligand-protein binding free en- ergy. Then, possible binding manners for 27 proteins of known crystal structures with hydrophobic ligands are simulated and analyzed via ICM flexible molecular docking and genetic algorithm, with re- sults greatly consistent with experimental values. By investigation, it is confirmed local hydrophobic effects of proteins and nonbinding/conformation interaction between ligand and protein both notably influence HIC chromatogram retention behaviors, mainly focusing on exposed portions on the protein surface. |
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| Keywords: | hydrophobic interaction chromatography flexible molecular docking genetic algorithm protein salting-in factor |
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