New insight into the binding interaction of hydroxylated carbon nanotubes with bovine serum albumin

Spectrochimica Acta - Part A: Molecular and Biomolecular Spectroscopy

Volumn 124, Issue , 2014, Pages 556-563

  Guan, Yonghui ^a   Zhang, Hongmei ^a   Wang, Yanqing ^a  

^a YANCHENG TEACHERS UNIVERSITY   (China)

Author keywords

Binding mechanism; Bovine serum albumin; Conformational changes; Fluorescence spectroscopy; Multi walled hydroxylated carbon nanotubes

Indexed keywords

BINDING MECHANISMS; BOVINE SERUM ALBUMINS; CHEMICAL DENATURATION; CONFORMATIONAL CHANGE; FLUORESCENCE INTENSITIES; SECONDARY STRUCTURES; STRUCTURAL STABILITIES; STRUCTURES AND PROPERTIES;

BINDING ENERGY; BODY FLUIDS; FLUORESCENCE SPECTROSCOPY; HYDROXYLATION; LIGANDS; MAMMALS; PROTEINS; STABILITY;

CARBON NANOTUBES;

BOVINE SERUM ALBUMIN; CARBON NANOTUBE; GUANIDINE; PROTEIN AGGREGATE; PROTEIN BINDING; THIAZOLE DERIVATIVE; THIOFLAVINE;

ANIMAL; BOVINE; CHEMISTRY; CIRCULAR DICHROISM; DRUG EFFECTS; HYDROXYLATION; KINETICS; METABOLISM; MOLECULAR DOCKING; PH; PROTEIN DENATURATION; PROTEIN SECONDARY STRUCTURE; SPECTROFLUOROMETRY;

ANIMALS; CATTLE; CIRCULAR DICHROISM; GUANIDINE; HYDROGEN-ION CONCENTRATION; HYDROXYLATION; KINETICS; MOLECULAR DOCKING SIMULATION; NANOTUBES, CARBON; PROTEIN AGGREGATES; PROTEIN BINDING; PROTEIN DENATURATION; PROTEIN STRUCTURE, SECONDARY; SERUM ALBUMIN, BOVINE; SPECTROMETRY, FLUORESCENCE; THIAZOLES;

EID: 84893564274     PISSN: 13861425     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.saa.2014.01.058     Document Type: Article

References (28)

1. D. Richards, and A. Ivanisevic Chem. Soc. Rev. 41 2012 2052 2060
2. L. Cao, X. Wang, M.J. Meziani, F. Lu, H. Wang, P.G. Luo, Y. Lin, B.A. Harruff, L.M. Veca, D. Murray, S.Y. Xie, and Y.P. Sun J. Am. Chem. Soc. 129 2007 11318 11319
3. T.W. Kim, P.W. Chung, I.I. Slowing, M. Tsunoda, E.S. Yeung, and V.S. Lin Nano Lett. 8 2008 3724 3727
4. C. Thauvin, S. Rickling, P. Schultz, H. Celia, and S. Meunier Nat. Nanotechnol. 3 2008 743 748
5. P. Roach, D. Farrar, and C.C. Perry J. Am. Chem. Soc. 127 2005 8168 8173
6. F. Bomboi, F. Tardani, D. Gazzoli, A. Bonincontro, and C.L. Mesa Colloids Surf. B 108 2013 16 22
7. U. Kragh-Hansen Pharm. Rev. 33 1981 17 53
8. L.E. Valenti, P.A. Fiorito, C.D. García, and C.E. Giacomelli J. Colloids Interface Sci. 307 2007 349 356
9. L.L. Li, R. Lin, H. He, L. Jiang, and M.M. Gao Spectrochim. Acta. Part A. 105 2013 45 51
10. M. Lundqvist, J. Stigler, G. Elia, I. Lynch, T. Cedervall, and K.A. Dawson Proc. Natl. Acad. Sci. USA 105 2008 14265 14270
11. E. Herczenik, and M.F.B.G. Gebbink FASEB J. 22 2008 2115 2133
12. S. Linse, C. Cabaleiro-Lago, W.F. Xue, I. Lynch, S. Lindman, E. Thulin, S.E. Radford, and K.A. Dawson Proc. Natl. Acad. Sci. USA 104 2007 8691 8696
13. G. Böhm, R. Muhr, and R. Jaenicke Protein Eng. 5 1992 191 195
14. Accelrys Inc. InsightII 2000 and Materials Studio, San Diego, CA.
15. .
16. .
17. .
18. F. Cañaveras, R. Madueño, J.M. Sevilla, M. Blázquez, and T. Pineda J. Phys. Chem. C 116 2012 10430 10437
19. X. Zhao, R. Liu, Z. Chi, Y. Teng, and P. Qin J. Phys. Chem. B 111 2010 5625 5631
20. F. Ding, J.X. Diao, Y. Sun, and Y. Sun J. Agric. Food. Chem. 60 2012 7218 7228
21. Z. Chi, R. Liu, and H. Zhang Biomacromolecules 11 2010 2454 2459
22. D.I. Cattoni, S.B. Kaufman, and F.L.G. Flecha Biochim. Biophys. Acta 1794 2009 1700 1708
23. J. Juárez, S.G. López, A. Cambón, P. Taboada, and V. Mosquera J. Phys. Chem. B 113 2009 10521 10529
24. N.K. Pandey, S. Ghosh, and S. Dasgupta J. Phys. Chem. B 114 2010 10228 10233
25. N.K. Holm, S.K. Jespersen, L.V. Thomassen, T.Y. Wolff, P. Sehgal, L.A. Thomsen, G. Christiansen, C.B. Andersen, A.D. Knudsen, and D.E. Otzen Biochim. Biophys. Acta 1774 2007 1128 1138
26. B. Ahmad, M.Z. Ahmed, S.K. Haq, and R.H. Khan Biochim. Biophys. Acta 1750 2005 93 102
27. H. Gao, X. Geng, B. Wang, and Y. Zhou J. Colloids Interface Sci. 344 2010 468 474
28. D. Shortle J. Biol. Chem. 264 1989 5315 5318