气候变化领域集成服务门户(CCPortal): Quantitative measurements of protein−surface interaction thermodynamics

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DOI	10.1073/pnas.1800287115
	Quantitative measurements of protein−surface interaction thermodynamics
	Kurnik M.; Ortega G.; Dauphin-Ducharme P.; Li H.; Caceres A.; Plaxco K.W.
发表日期	2018
ISSN	0027-8424
起始页码	8352
结束页码	8357
卷号	115 期号:33
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.
英文关键词	Biophysics; Biosensors; Protein folding; Protein−surface interactions; Square wave voltammetry
语种	英语
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
来源期刊	Proceedings of the National Academy of Sciences of the United States of America
文献类型	期刊论文
条目标识符	http://gcip.llas.ac.cn/handle/2XKMVOVA/160482
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 Ce...
推荐引用方式 GB/T 7714	Kurnik M.,Ortega G.,Dauphin-Ducharme P.,et al. Quantitative measurements of protein−surface interaction thermodynamics[J],2018,115(33).
APA	Kurnik M.,Ortega G.,Dauphin-Ducharme P.,Li H.,Caceres A.,&Plaxco K.W..(2018).Quantitative measurements of protein−surface interaction thermodynamics.Proceedings of the National Academy of Sciences of the United States of America,115(33).
MLA	Kurnik M.,et al."Quantitative measurements of protein−surface interaction thermodynamics".Proceedings of the National Academy of Sciences of the United States of America 115.33(2018).