NMR studies on binding sites and aggregation-disassociation of fluorinated surfactant sodium perfluorooctanoate on protein ubiquitin

Biochimica et Biophysica Acta - General Subjects

Volumn 1790, Issue 2, 2009, Pages 134-140

  Lu, Run Chao ^a   Guo, Xian Rong ^a,b   Jin, Changwen ^a,b   Xiao, Jin Xin ^a,c  

^a PEKING UNIVERSITY   (China)

^b Beijing Nuclear Magnetic Resonance Center   (China)

^c Beijing FLUOBON Surfactant Institute   (China)

Author keywords

Binding sites; Dodecyltrimethylammonium chloride; Sodium perfluorooctanoate; Ubiquitin; Unfolding

Indexed keywords

NITROGEN 15; SODIUM PERFLUOROOCTANOATE; SURFACTANT; UBIQUITIN PROTEIN LIGASE; UNCLASSIFIED DRUG;

ARTICLE; BINDING SITE; CHEMICAL LABELING; CHEMICAL STRUCTURE; COMPLEX FORMATION; CONCENTRATION RESPONSE; DISSOCIATION; FLUORINE NUCLEAR MAGNETIC RESONANCE; HETERONUCLEAR SINGLE QUANTUM COHERENCE; MICELLIZATION; PRIORITY JOURNAL; PROTEIN AGGREGATION; PROTEIN BINDING; PROTEIN FOLDING;

BINDING SITES; FLUOROCARBONS; MODELS, BIOLOGICAL; MODELS, MOLECULAR; NUCLEAR MAGNETIC RESONANCE, BIOMOLECULAR; OCTANOIC ACIDS; PRECIPITATION; PROTEIN BINDING; PROTEIN FOLDING; SURFACE-ACTIVE AGENTS; UBIQUITIN;

EID: 58149187915     PISSN: 03044165     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.bbagen.2008.10.009     Document Type: Article

References (18)

1. Deep S., and Ahluwalia J.C. Interaction of bovine serum albumin with anionic surfactants. Phys. Chem. 3 (2001) 4583-4591
2. Ananthapadmanabhan K.P. Protein-surfactant interactions. In: Goddard E.D., and Ananthapadmanabhan K.P. (Eds). Interactions of Surfactants with Polymers and Proteins (1993), CRC Press, London 319-365
3. Otzen D.E. Protein unfolding in detergents: effect of micelle structure, ionic strength, pH, and temperature. Biophys. J. 83 (2002) 2219-2230
4. Sun C.X., Yang J.H., Wu X., Huang X.R., Wang F., and Liu S.F. Unfolding and refolding of bovine serum albumin induced by cetylpyridinium bromide. Biophys. J. 88 (2005) 3518-3524
5. Lu R.-C., Xiao J.-X., Cao A.-N., and Lai L.-H. Effect of cationic surfactants on the interaction between sodium perfluorooctanoate and β-lactoglobulin. J. Colloid Interface Sci. 293 (2006) 61-69
6. Lu R.-C., Cao A.-N., Lai L.-H., and Xiao J.-X. Protein-surfactant interaction: differences between fluorinated and hydrogenated surfactants. Colloid Surf., B Biointerfaces 64 (2008) 98-103
7. Xing H., Lin S.-S., Yan P., Xiao J.-X., and Chen Y.-M. NMR studies on selectivity of β-cyclodextrin to fluorinated/hydrogenated surfactant mixtures. J. Phys. Chem., B 111 (2007) 8089-8095
8. Delaglio F., Grzesiek S., Vuister G.W., Zhu G., Pfeifer J., and Bax A. NMR pipe: a multidimensional spectral processing system based on UNIX pipes. J. Biomol. NMR 6 (1995) 277-293
9. Johnson B.A. Using NMR view to visualize and analyze the NMR spectra of macromolecules. Methods Mol. Biol. 278 (2004) 313-352
10. Vijay-Kumar S., Bugg C.E., and Cook W.J. Comparison of the three-dimensional structures of human, yeast, and oat ubiquitin. J. Mol. Biol. 194 (1987) 531-544
11. Di Stefano D.L., and Wand A.J. Two-dimensional proton NMR study of human ubiquitin: a main chain directed assignment and structure analysis. Biochemistry 26 (1987) 7272-7290
12. Irbäck A., Mitternacht S., and Mohanty S. Dissecting the mechanical unfolding of ubiquitin. Proc. Natl. Acad. Sci. 102 (2005) 13427-13432
13. Lu R.-C., Xiao J.-X., Cao A.-N., Lai L.-H., Zhu B.-Y., and Zhao G.-X. Surfactant-induced refolding of lysozyme. Biochim. Biophys. Acta-Gen. Subj. 1722 (2005) 271-281
14. Makhatadze G.I., Loladze V.V., Ermolenko D.N., Chen X.F., and Thomas S.T. Anion binding to the ubiquitin molecule. J. Mol. Biol. 327 (2003) 1135-1148
15. Sundd M., and Robertson A.D. Electrostatic interactions in ubiquitin: stabilization of carboxylates by lysine amino groups. J. Mol. Biol. 332 (2003) 927-936
16. Loladze V.V., and Makhatadze G.I. Removal of surface charge-charge interactions from ubiquitin leaves the protein folded and very stable. Protein Sci. 11 (2002) 174-177
17. Zhao G.-X., and Zhu B.-Y. Surfactant adsorption and aggregation. J. Disper. Sci. Technol. 16 (1995) 305-332
18. Wand A.J., Ehrhardt M.R., and Flynn P.F. High-resolution NMR of encapsulated proteins dissolved in low-viscosity fluids. Biophysics 95 (1998) 15299-15302