globalchange  > 气候变化与战略
DOI: 10.1073/pnas.1800287115
论文题名:
Quantitative measurements of protein−surface interaction thermodynamics
作者: Kurnik M.; Ortega G.; Dauphin-Ducharme P.; Li H.; Caceres A.; Plaxco K.W.
刊名: Proceedings of the National Academy of Sciences of the United States of America
ISSN: 0027-8424
出版年: 2018
卷: 115, 期:33
起始页码: 8352
结束页码: 8357
语种: 英语
英文关键词: Biophysics ; Biosensors ; Protein folding ; Protein−surface interactions ; Square wave voltammetry
Scopus关键词: protein kinase Fyn ; protein SH3 ; FYN protein, human ; protein kinase Fyn ; Article ; bacterial cell ; biocompatibility ; controlled study ; molecular stability ; nonhuman ; polyacrylamide gel electrophoresis ; priority journal ; protein analysis ; protein interaction ; protein structure ; quantitative analysis ; sequence analysis ; static electricity ; thermodynamics ; chemistry ; electrochemical analysis ; human ; protein folding ; protein stability ; Src homology domain ; Electrochemical Techniques ; Humans ; Protein Folding ; Protein Stability ; Proto-Oncogene Proteins c-fyn ; src Homology Domains ; Thermodynamics
英文摘要: Whereas proteins generally remain stable upon interaction with biological surfaces, they frequently unfold on and adhere to artificial surfaces. Understanding the physicochemical origins of this discrepancy would facilitate development of protein-based sensors and other technologies that require surfaces that do not compromise protein structure and function. To date, however, only a small number of such artificial surfaces have been reported, and the physics of why these surfaces support functional biomolecules while others do not has not been established. Thus motivated, we have developed an electrochemical approach to determining the folding free energy of proteins site-specifically attached to chemically well-defined, macroscopic surfaces. Comparison with the folding free energies seen in bulk solution then provides a quantitative measure of the extent to which surface interactions alter protein stability. As proof-of-principle, we have characterized the FynSH3 domain site-specifically attached to a hydroxyl-coated surface. Upon guanidinium chloride denaturation, the protein unfolds in a reversible, two-state manner with a free energy within 2 kJ/mol of the value seen in bulk solution. Assuming that excluded volume effects stabilize surface-attached proteins, this observation suggests there are countervening destabilizing interactions with the surface that, under these conditions, are similar in magnitude. Our technique constitutes an unprecedented experimental tool with which to answer long-standing questions regarding the molecular-scale origins of protein−surface interactions and to facilitate rational optimization of surface biocompatibility. © 2018 National Academy of Sciences. All rights reserved.
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资源类型: 期刊论文
标识符: http://119.78.100.158/handle/2HF3EXSE/163678
Appears in Collections:气候变化与战略

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作者单位: Kurnik, M., Department of Chemistry and Biochemistry, University of California, Santa Barbara, CA 93106, United States, Center for Bioengineering, University of California, Santa Barbara, CA 93106, United States; Ortega, G., Department of Chemistry and Biochemistry, University of California, Santa Barbara, CA 93106, United States, Center for Bioengineering, University of California, Santa Barbara, CA 93106, United States, Protein Stability and Inherited Disease Laboratory, Center for Cooperative Research, Biosciences CIC bioGUNE, Derio, 48170, Spain; Dauphin-Ducharme, P., Department of Chemistry and Biochemistry, University of California, Santa Barbara, CA 93106, United States, Center for Bioengineering, University of California, Santa Barbara, CA 93106, United States; Li, H., Department of Chemistry and Biochemistry, University of California, Santa Barbara, CA 93106, United States, Center for Bioengineering, University of California, Santa Barbara, CA 93106, United States, Engineering Research Center of Nano-Geomaterials, Ministry of Education, Faculty of Materials Science and Chemistry, China University of Geosciences, Wuhan, 430074, China; Caceres, A., Department of Chemistry and Biochemistry, University of California, Santa Barbara, CA 93106, United States, Center for Bioengineering, University of California, Santa Barbara, CA 93106, United States; Plaxco, K.W., Department of Chemistry and Biochemistry, University of California, Santa Barbara, CA 93106, United States, Center for Bioengineering, University of California, Santa Barbara, CA 93106, United States

Recommended Citation:
Kurnik M.,Ortega G.,Dauphin-Ducharme P.,et al. Quantitative measurements of protein−surface interaction thermodynamics[J]. Proceedings of the National Academy of Sciences of the United States of America,2018-01-01,115(33)
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