Modulation of pathway of insulin fibrillation by a small molecule helix inducer 2,2,2-trifluoroethanol

Colloids and Surfaces B: Biointerfaces

Volumn 92, Issue , 2012, Pages 142-150

  Banerjee, Victor ^a   Das, K P ^a  

^a BOSE INSTITUTE   (India)

Author keywords

Insulin fibril morphology; Insulin fibrillation; Kinetics of fibrillation; Lag phase; Pathway of insulin fibrillation; Protofibrillar intermediates; Role of TFE

Indexed keywords

FIBRIL MORPHOLOGY; LAG PHASE; PATHWAY OF INSULIN FIBRILLATION; PROTOFIBRILLAR INTERMEDIATES; ROLE OF TFE;

ETHANOL; GLYCOPROTEINS; MOLECULES; NEURODEGENERATIVE DISEASES; OLIGOMERS; PROTEINS;

INSULIN;

BOVINE INSULIN; THIOFLAVINE; TRIFLUOROETHANOL;

ALPHA HELIX; ARTICLE; CHEMICAL REACTION KINETICS; CIRCULAR DICHROISM; CONFORMATIONAL TRANSITION; CONTROLLED STUDY; DRUG EFFECT; DRUG MECHANISM; HYDRODYNAMICS; IN VITRO STUDY; INFRARED SPECTROSCOPY; INSULIN FIBRILLATION; LIGHT SCATTERING; MOLECULAR INTERACTION; NONHUMAN; OLIGOMERIZATION; PH; PRIORITY JOURNAL; PROCESS OPTIMIZATION; PROTEIN AGGREGATION; PROTEIN MODIFICATION; PROTEIN SECONDARY STRUCTURE; TRANSMISSION ELECTRON MICROSCOPY; VISCOSITY;

AMYLOID; ANIMALS; CATTLE; CIRCULAR DICHROISM; HYDRODYNAMICS; HYDROGEN-ION CONCENTRATION; INSULIN; KINETICS; LIGHT; PARTICLE SIZE; PROTEIN STRUCTURE, QUATERNARY; PROTEIN STRUCTURE, SECONDARY; SCATTERING, RADIATION; SOLUTIONS; SPECTROMETRY, FLUORESCENCE; SPECTROSCOPY, FOURIER TRANSFORM INFRARED; TEMPERATURE; THIAZOLES; TIME FACTORS; TRIFLUOROETHANOL;

TRIFLUORO;

EID: 84856080052     PISSN: 09277765     EISSN: 18734367     Source Type: Journal    
DOI: 10.1016/j.colsurfb.2011.11.036     Document Type: Article

References (48)

1. Chiti F., Dobson C.M. Nat. Chem. Biol. 2009, 5:15.
2. Selkoe D.J. Nature 2003, 426:900.
3. Sumner Makin O., Serpell L.C. J. Mol. Biol. 2004, 335:1279.
4. Dobson C.M. Nature 2002, 418:729.
5. Stefani M., Dobson C. J. Mol. Med. 2003, 81:678.
6. Uversky V.N., Fink A.L. Biochim. Biophys. Acta - Proteins Proteomics 2004, 1698:131.
7. Sunde M., Blake C Adv. Protein Chem. 1997, 50:123.
8. Nelson R., Sawaya M.R., Balbirnie M., Madsen A.O., Riekel C., Grothe R., Eisenberg D. Nature 2005, 435:773-778.
9. Booth D.R., Sunde M., Bellotti V., Robinson C.V., Hutchinson W.L., Fraser P.E., Hawkins P.N., Dobson C.M., Radford S.E., Blake C.C.F., Pepys M.B. Nature 1997, 385:787.
10. Niraula T.N., Haraoka K., Ando Y., Li H., Yamada H., Akasaka K. J. Mol. Biol. 2002, 320:333.
11. Goldsbury C.S., Cooper G.J.S., Goldie K.N., Müller S.A., Saafi E.L., Gruijters W.T.M., Misur M.P., Engel A., Aebi U., Kistler J. J. Struct. Biol. 1997, 119:17.
12. Caughey B., Lansbury P.T. Annu. Rev. Neurosci. 2003, 26:267.
13. Bucciantini M., Giannoni E., Chiti F., Baroni F., Formigli L., Zurdo J., Taddei N., Ramponi G., Dobson C.M., Stefani M. Nature 2002, 416:507.
14. Kayed R., Head E., Thompson J.L., McIntire T.M., Milton S.C., Cotman C.W., Glabe C.G. Science 2003, 300:486.
15. Lambert M.P., Barlow A.K., Chromy B.A., Edwards C., Freed R., Liosatos M., Morgan T.E., Rozovsky I., Trommer B., Viola K.L., Wals P., Zhang C., Finch C.E., Krafft G.A., Klein W.L. Proc. Natl. Acad. Sci. U. S. A. 1998, 95:6448.
16. Jayaraman M., Kannayiram G., Rajadas J. Arch. Biochem. Biophys. 2008, 474:15.
17. Lasagna-Reeves C.A., Clos A.L., Midoro-Hiriuti T., Goldblum R.M., Jackson G.R., Kayed R. Endocrinology 2010, 151:4717.
18. Blundell T.L., Cutfield J.F., Cutfield S.M., Dodson E.J., Dodson G.G., Hodgkin D.C., Mercola D.A., Vijayan M. Nature 1971, 231:506.
19. Brange J., Andersen L., Laursen E.D., Meyn G., Rasmussen E. J. Pharm. Sci. 1997, 86:517.
20. Waugh D.F. J. Am. Chem. Soc. 1946, 68:247.
21. Ahmad A., Uversky V.N., Hong D., Fink A.L. J. Biol. Chem. 2005, 280:42669.
22. Bouchard M., Zurdo J., Nettleton E.J., Dobson C.M., Robinson C.V. Protein Sci. 2000, 9:1960.
23. Tang Q., Solin N., Lu J., Inganas O. Chem. Commun. 2010, 46:4157.
24. Jiménez J.L., Nettleton E.J., Bouchard M., Robinson C.V., Dobson C.M., Saibil H.R. Proc. Natl. Acad. Sci. U. S. A. 2002, 99:9196.
25. Sonnichsen F.D., Van Eyk J.E., Hodges R.S., Sykes B.D. Biochemistry 1992, 31:8790.
26. Hirota N., Goto Y., Mizuno K. Protein Sci. 1997, 6:416.
27. Arunkumar A.I., Kumar T.K.S., Yu C. Int. J. Biol. Macromol. 1997, 21:223.
28. Grudzielanek S., Jansen R., Winter R. J. Mol. Biol. 2005, 351:879.
29. Buck M. Q. Rev. Biophys. 1998, 31:297.
30. Ecroyd H., Carver J. Cell. Mol. Life Sci. 2009, 66:62.
31. Liu W., Prausnitz J.M., Blanch H.W. Biomacromolecules 2004, 5:1818.
32. Vieira E.P., Hermel H., Möhwald H. Biochim. Biophys. Acta - Proteins Proteomics 2003, 1645:6.
33. Nayak A., Sorci M., Krueger S., Belfort G. Proteins Struct. Funct. Bioinform. 2009, 74:556.
34. Praissman M., Rupley J.A. Biochemistry 1968, 7:2431.
35. Groenning M., Olsen L., van de Weert M., Flink J.M., Frokjaer S., Jørgensen F.S. J. Struct. Biol. 2007, 158:358.
36. Nilsson M.R., Dobson C.M. Protein Sci. 2003, 12:2637.
37. Levine H. Protein Sci. 1993, 2:404.
38. Naiki H.H.K., Nakakuki K., Takeda T. Lab. Invest. 1991, 65:104.
39. Lide D.R.e. CRC Handbook of Chemistry and Physics 1999, CRC Press. 80th ed.
40. Vestergaard B., Groenning M., Roessle M., Kastrup J.S., de Weert M.v., Flink J.M., Frokjaer S., Gajhede M., Svergun D.I. PLoS Biol. 2007, 5:e134.
41. Nielsen L., Khurana R., Coats A., Frokjaer S., Brange J., Vyas S., Uversky V.N., Fink A.L. Biochemistry 2001, 40:6036.
42. Jeffrey P.D., Coates J.H. Biochemistry 1966, 5:489.
43. Surewicz W.K., Mantsch H.H., Chapman D. Biochemistry 1993, 32:389.
44. Dong A., Matsuura J., Allison S.D., Chrisman E., Manning M.C., Carpenter J.F. Biochemistry 1996, 35:1450.
45. Sekhar A., Udgaonkar J.B. Biochemistry 2010, 50:805.
46. Yamaguchi K.-i., Naiki H., Goto Y. J. Mol. Biol. 2006, 363:279.
47. Hong D.-P., Hoshino M., Kuboi R., Goto Y. J. Am. Chem. Soc. 1999, 121:8427.
48. Kumar S., Modig K., Halle B. Biochemistry 2003, 42:13708.