Effect of (-)-epigallocatechin gallate on the fibrillation of human serum albumin

International Journal of Biological Macromolecules

Volumn 70, Issue , 2014, Pages 312-319

  Bhattacharya, Susmita ^a   Pandey, Nitin K ^a   Roy, Anushree ^a   Dasgupta, Swagata ^a  

^a INDIAN INSTITUTE OF TECHNOLOGY   (India)

Author keywords

( ) Epigallocatechin gallate; Fibrillation; Human serum albumin; Spectroscopy

Indexed keywords

EPIGALLOCATECHIN GALLATE; HUMAN SERUM ALBUMIN; TRYPTOPHAN; CATECHIN; PROTEIN BINDING; SERUM ALBUMIN; TEA;

ANISOTROPY; ARTICLE; BINDING AFFINITY; CONTROLLED STUDY; DRUG MECHANISM; DRUG PROTEIN BINDING; DRUG STRUCTURE; FLUORESCENCE ANALYSIS; RAMAN SPECTROMETRY; ANALOGS AND DERIVATIVES; CHEMICAL STRUCTURE; CHEMISTRY; HUMAN; METABOLISM; PROTEIN CONFORMATION; TEA;

CATECHIN; HUMANS; MODELS, MOLECULAR; PROTEIN BINDING; PROTEIN CONFORMATION; SERUM ALBUMIN; TEA;

EID: 84904916216     PISSN: 01418130     EISSN: 18790003     Source Type: Journal    
DOI: 10.1016/j.ijbiomac.2014.07.003     Document Type: Article

References (50)

1. Pandey K.B., Rizvi S.I. Oxid. Med. Cell. Longev. 2009, 2:270-278.
2. Wang Z.Y., Huang M.T., Lou Y.R., Xie J.G., Reuhl K.R., Newmark H.L., Ho C.T., Yang C.S., Conney A.H. Cancer Res. 1994, 54:3428-3435.
3. Higdon J.V., Frei B. Crit. Rev. Food. Sci. 2003, 43:89-143.
4. Nanjo F., Goto K., Seto R., Suzuki M., Sakai M., Hara Y. Free Radic. Biol. Med. 1996, 21:895-902.
5. Singh M., Arseneault M., Sanderson T., Murthy V., Ramassamy C. J. Agric. Food Chem. 2008, 56:4855-4873.
6. Howett D.R., George A.R., Owen D.E., Ward R.V., Markel R.E. Biochem. J. 1999, 343:419-423.
7. Meng X., Munishkina L.A., Fink A.L., Uversky V.N. Biochemistry 2009, 48:8206-8224.
8. Bieschke J., Russ J., Friedrich R.P., Ehrnhoefer D.E., Wobst H., Neugebauer K., Wanker E.E. Proc. Natl. Acad. Sci. U.S.A. 2010, 107:7710-7715.
9. Yang F., Lim G.P., Begum A.N., Ubeda O.J., Simmons M.R., Ambegaokar S.S., Chen P.P., Kayed R., Glabe C.G., Frautschy S.A., Cole G.M. J. Biol. Chem. 2005, 280:5892-5901.
10. Engel M.F., vandenAkker C.C., Schleeger M., Velikov K.P., Koenderink G.H., Bonn M. J. Am. Chem. Soc. 2012, 134:14781-14788.
11. Palhano F.L., Lee J., Grimster N.P., Kelly J.W. J. Am. Chem. Soc. 2013, 135:7503-7510.
12. He X.M., Carter D.C. Nature 1992, 358:209-215.
13. Sugio S., Kashima A., Mochizuki S., Noda M., Kobayashi K. Protein Eng. 1999, 12:439-446.
14. Miškovský P., Jancura D., Sánchez-Cortés S., Kočišová E., Chinsky L. J. Am. Chem. Soc. 1998, 120:6374-6379.
15. Dockal M., Carter D.C., Ruker F. J. Biol. Chem. 2000, 275:3042-3050.
16. Hasimoto S., Yabusaki T., Takeuchi H., Harada I. Biospectroscopy 1995, 1:375-385.
17. Alberts B., Johnson A., Lewis J. Molecular Biology of the Cell 2002, Garland Science, New York. 4th ed.
18. Farruggia B., Rodriguez F., Rigatuso R., Fidelio G., Pico G. J. Protein Chem. 2001, 20:81-89.
19. Flora K., Brennan J.D., Baker G.A., Doody M.A., Bright F.V. Biophys. J. 1998, 75:1084-1096.
20. Taboada P., Barbosa S., Castro E., Gutiérrez-Pichel M., Mosquera V. Chem. Phys. 2007, 340:59-68.
21. Stepuro I.I., Lapshina E.A., Chaikovskaia N.A. Mol. Biol. (Moscow) 1991, 25:337-347.
22. Taboada P., Barbosa S., Castro E., Mosquera V. J. Phys. Chem. B 2006, 110:20733-20736.
23. Juárez J., Taboada P., Mosquera V. Biophys. J. 2009, 96:2353-2370.
24. Juárez J., Goy-Lopez S., Cambon A., Taboada P., Mosquera V. J. Phys. Chem. B 2009, 113:10521-10529.
25. Juárez J., Taboada P., Goy-Lopez S., Cambon A., Madec M.B., Yeates S.G., Mosquera V. J. Phys. Chem. B 2009, 113:12391-12399.
26. Juárez J., Alatorre-Meda M., Cambón A., Topete A., Barbosa S., Taboada P., Mosquera V. Soft Matter 2012, 8:3608-3619.
27. Stirpe A., Pantusa M., Rizzuti B., Sportelli L., Bartucci R., Guzzi R. Int. J. Biol. Macromol. 2011, 49:337-342.
28. Vannoy C.H., Leblanc R.M. J. Phys. Chem. B 2010, 114:10881-10888.
29. Goy-Lopez S., Juárez J., Manuel A.M., Casals E., Puntes V.F., Taboada P., Mosquera V. Langmuir 2012, 28:9113-9126.
30. Pandey N.K., Ghosh S., Dasgupta S. J. Phys. Chem. B 2010, 114:10228-10233.
31. Pace C.N., Vajdos F., Fee L., Grimsley G., Gray T. Protein Sci. 1995, 4:2411-2423.
32. Conchillo-Solé O., de Groot N.S., Avilés F.X., Vendrell J., Daura X., Ventura S. BMC Bioinformatics 2007, 8:65-83.
33. Vanwart H.E., Lewis A., Scheraga H.A., Saevat F.D. Proc. Natl. Acad. Sci. U.S.A. 1973, 70:2619-2623.
34. Schmid F.X. Encyclopedia of Life Sciences 2001, 1-4. Macmillan Publishers Ltd., London, UK.
35. Kuntz I.D., Gasparro F.P., Johnston M.D., Taylor R.P. J. Am. Chem. Soc. 1968, 90:4778-4782.
36. Maiti T.K., Ghosh K.S., Dasgupta S. Proteins 2006, 64:355-362.
37. Tuma R. J. Raman Spectrosc. 2005, 36:307-319.
38. Ishizaki H., Balaram P., Nagaraj R., Venkatachalapathi Y.V., Tu A.T. Biophys. J. 1981, 36:509-517.
39. Bhattacharya S., Ghosh S., Pandey N.K., Chaudhury S., Dasgupta S., Roy A. J. Phys. Chem. B 2013, 117:13993-14000.
40. Schweitzer-Stenner R. J. Phys. Chem. B 2012, 116:4141-4153.
41. Xu M., Shashilov V., Lednev I.K. J. Am. Chem. Soc. 2007, 129:11002-11003.
42. Meng F., Abedini A., Plesner A., Verchere C.B., Raleigh D.P. Biochemistry 2010, 49:8127-8133.
43. Neilson A.P., Ferruzzi M.G. Annu. Rev. Food Sci. Technol. 2011, 2:125-151.
44. Lakowicz J.R. Principles of Fluorescence Spectroscopy 2009, 353-370. Kluwer Academic/Plenum Publishers, New York, Boston, Dordrecht, London, Moscow. 3rd ed.
45. Inouye H., Sharma D., Goux W.J., Kirschner D.A. Biophys. J. 2006, 90:1774-1789.
46. Tycko R. Q. Rev. Biophys. 2006, 39:1-55.
47. Su Y., Sarell C.J., Eddy M.T., Debelouchina G.T., Andreas L.B., Pashley C.L., Radford S.E., Griffin R.G. J. Am. Chem. Soc. 2014, 136:6313-6325.
48. Kubinyi M., Billesl F., Grofcsik A., Keresztury G. J. Mol. Struct. 1992, 266:339-344.
49. Song L.-L., Liang R., Li D.-D., Xing Y.-D., Han R.-M., Zhang J.-P., Skibsted L.H. J. Agric. Food Chem. 2011, 59:12643-12651.
50. Machado N.F.L., Calheiros R., Gaspar A., Garrido J., Borgesa F., Marques M.P.M. J. Raman Spectrosc. 2009, 40:80-85.