Human insulin fibril-assisted synthesis of fluorescent gold nanoclusters in alkaline media under physiological temperature

Colloids and Surfaces B: Biointerfaces

Volumn 105, Issue , 2013, Pages 167-172

  Garcia, Andrew R ^a   Rahn, Ivy ^a   Johnson, Sheba ^a   Patel, Ravi ^a   Guo, Jingru ^a   Orbulescu, Jhony ^a,b   Micic, Miodrag ^b,c   Whyte, Jeffrey D ^b   Blackwelder, Patricia ^d   Leblanc, Roger M ^a  

^a Department of Biology   (United States)

^b MP Biomedicals LLC   (United States)

^c Cerritos College   (United States)

^d UNIVERSITY OF MIAMI   (United States)

Author keywords

Biomacromolecular assembly; Fibrillation; Insulin; Materials chemistry; Nanoclusters; Photonics

Indexed keywords

ALKALINE MEDIA; ALKALINE MEDIUM; FIBRIL STRUCTURE; FIBRILLATION; GOLD NANOCLUSTER; GRAPHICAL DESCRIPTION; MATERIALS CHEMISTRY; NANOCLUSTER FORMATION; OPTIMIZED SYNTHESIS; PHYSIOLOGICAL TEMPERATURE; SYNTHETIC APPROACH; SYNTHETIC PROCEDURES;

ALKALINITY; EXPERIMENTS; FLUORESCENCE; GOLD; NANOCLUSTERS; PHOTONICS; PHYSIOLOGY; PROTEINS;

INSULIN;

FLUORESCENT INSULIN FIBRIL GOLD NANOCLUSTER; GOLD NANOPARTICLE; INSULIN; UNCLASSIFIED DRUG;

AQUEOUS SOLUTION; ARTICLE; CONTROLLED STUDY; FLUORESCENCE SPECTROSCOPY; HEATING; MICROSCOPY; PRIORITY JOURNAL; SYNTHESIS; TEMPERATURE; ULTRAVIOLET SPECTROSCOPY;

CHLORIDES; CULTURE MEDIA; FLUORESCENCE; GOLD; GOLD COMPOUNDS; HUMANS; INSULIN; METAL NANOPARTICLES; MICROSCOPY, ATOMIC FORCE; SPECTROPHOTOMETRY, ULTRAVIOLET; TEMPERATURE; TOMOGRAPHY, X-RAY COMPUTED; WATER;

EID: 84873192219     PISSN: 09277765     EISSN: 18734367     Source Type: Journal    
DOI: 10.1016/j.colsurfb.2012.12.052     Document Type: Article

References (25)

1. Dabbousi B.O., Rodriguez-Viejo J., Mikulec F.V., Heine J.R., Mattoussi H., Ober R., Jensen K.F., Bawendi M.G. J. Phys. Chem. B 1997, 101:9463-9475.
2. Lee T.-H., Gonzales J.I., Zheng J., Dickson R.M. Acc. Chem. Res. 2005, 38:534-541.
3. Suzdalev I.P., Suzdalev P.I. Russ. Chem. Rev. 2001, 70:177-210.
4. Kawasaki H., Hamaguchi K., Osaka I., Arakawa R. Adv. Funct. Mater. 2011, 21:3508-3515.
5. Xie J., Zheng Y., Ying J.Y. J. Am. Chem. Soc. 2009, 131:888-889.
6. Liu C.-L., Hsiao Y.-H., Lai C.-W., Shih C.-W., Peng Y.-K., Tang K.-C., Chang H.-W., Chou P.-T. Angew. Chem. Int. Ed. 2011, 50:7056-7060.
7. Saltiel A.R., Kahn C.R. Nature 2001, 414:799-806.
8. Nettleton E.J., Tito P., Sunde M., Bouchard M., Dobson C.M., Robinson C.V. Biophys. J. 2000, 79:1053-1065.
9. Pocker Y., Biswas S.B. Biochemistry 1980, 19:5043-5049.
10. Hua Q.-X Protein Cell 2010, 1:537-551.
11. Brange J., Andersen L., Laursen E.D., Meyn G., Rasmussen E. J. Pharm. Sci. 1997, 86:517-525.
12. Jansen R., Dzwolak W., Winter R. Biophys. J. 2005, 88:1344-1353.
13. Lee C.-C., Nayak A., Sethuraman A., Belfort G., McRae G.J. Biophys. J. 2007, 92:3448-3458.
14. Librizzi F., Rischel C. Protein Sci. 2005, 14:3129-3134.
15. Helmerhorst E., Stokes G.B. Diabetes 1987, 36:261-264.
16. Waugh D.F., Smith M.J., Fearing D.F. Fed. Proc. 1948, 7:131.
17. Waugh D.F. J. Am. Chem. Soc. 1948, 70:1850-1857.
18. Guo S., Akhremitchev B.B. Langmuir 2008, 24:880-887.
19. Nielsen L., Frokjaer S., Brange J., Uversky V.N., Fink A.L. Biochemistry 2001, 40:8397-8409.
20. Muzzafar M., Ahmad A. PloS ONE 2011, 6(11):1-11.
21. Klement K., Wieligmann K., Meinhardt J., Hortschansky P., Richter W., Fandrich M. J. Mol. Biol. 2007, 373:1321-1333.
22. Gras S.L., Waddington L.J., Goldie K.N. Methods Mol. Biol. 2011, 752:197-214.
23. Siposova K., Kubovcikova M., Bednarikova Z., Koneracka M., Zavisova V., Antosova A., Kopcansky P., Daxnerova Z., Gazova Z. Nanotechnology 2012, 23:1-10.
24. Brange J., Ribel U., Hansen J.F., Dodson G., Hansen M.T., Havelund S., Melberg S.G., Norris F., Norris K., Snel L., Sørensen A.R., Voigt H.O. Nature 1988, 333:679-682.
25. Graham J.S., Miron Y., Gradbois M. J. Mol. Recognit. 2011, 24:477-482.