Surface chemistry at the nanometer scale influences insulin aggregation

Colloids and Surfaces B: Biointerfaces

Volumn 100, Issue , 2012, Pages 69-76

  Pandey, Lalit M ^a,c   Le Denmat, Simon ^b   Delabouglise, Didier ^a   Bruckert, Franz ^a   Pattanayek, Sudip K ^c   Weidenhaupt, Marianne ^a  

^a LABORATOIRE DES MATÉRIAUX ET DU GÉNIE PHYSIQUE   (France)

^b Centre Interuniversitaire de MicroElectronique et Nanotechnologies (CIME Nanotech)   (France)

^c INDIAN INSTITUTE OF TECHNOLOGY DELHI   (India)

Author keywords

Insulin; Material roughness; Protein aggregation; Self assembled monolayers (SAMs); Wettability

Indexed keywords

ADSORPTION RATES; AGGREGATION KINETICS; AGGREGATION PROCESS; GROWTH PHASE; LAG PHASE; LAG-TIME; MATERIAL SURFACE; NANO-METER SCALE; OCTYL GROUPS; PROTEIN ADSORPTION; PROTEIN AGGREGATION; SECONDARY STRUCTURES;

ADSORPTION; AGGLOMERATION; AGGREGATES; INSULIN; ORGANIC COMPOUNDS; PROTEINS; SELF ASSEMBLED MONOLAYERS; SURFACE CHEMISTRY; SURFACE ROUGHNESS; WETTING;

SURFACES;

AMINE; INSULIN; OCTYL SILANE; UNCLASSIFIED DRUG;

ADSORPTION; ARTICLE; CHEMICAL COMPOSITION; CHEMICAL STRUCTURE; CONTROLLED STUDY; GROWTH RATE; HYDROPHOBICITY; KINETICS; LAG; PHYSICAL PARAMETERS; PRIORITY JOURNAL; PROTEIN AGGREGATION; ROUGHNESS; SURFACE CHEMISTRY; SURFACE PROPERTY; SYNTHESIS;

ADSORPTION; COATED MATERIALS, BIOCOMPATIBLE; FLUORESCENT DYES; GLASS; HUMANS; HYDROPHOBIC AND HYDROPHILIC INTERACTIONS; INSULIN; KINETICS; MICROSCOPY, ATOMIC FORCE; NANOSTRUCTURES; PROTEIN STRUCTURE, SECONDARY; RECOMBINANT PROTEINS; SILANES; SPECTROMETRY, FLUORESCENCE; SPECTROSCOPY, FOURIER TRANSFORM INFRARED; SURFACE PROPERTIES; THIAZOLES;

EID: 84863211329     PISSN: 09277765     EISSN: 18734367     Source Type: Journal    
DOI: 10.1016/j.colsurfb.2012.05.022     Document Type: Article

References (24)

1. Selkoe D.J. Ann. N.Y. Acad. Sci. 2000, 924:17.
2. Yankner B.A. Neuron 1996, 16:921.
3. Guela C., Wu C.K., Saroff D., Lorenzo A., Yuan M., Yankner B.A. Nat. Med. 1998, 4:827.
4. Perutz M.F. Curr. Opin. Struct. Biol. 1996, 6:848.
5. Prusiner S.B. Trends Biochem. Sci. 1996, 21:482.
6. Rousseau F., Schymkowitz1 J., Serrano L. Curr. Opin. Struct. Biol. 2006, 16:118.
7. Sluzky V., Tamada J.A., Klibanovt A.M., Langer R. Proc. Natl. Acad. Sci. U.S.A. 1991, 88:9377.
8. Whittingham J.L., Scott D.J., Chance K., Wilson A., Finch J., Brange J., Dodson G.G. J. Mol. Biol. 2002, 318:479.
9. Ivanova M.I., Sievers S.A., Sawaya M.R., Wall J.S., Eisenberg D. Proc. Natl. Acad. Sci. U.S.A. 2009, 106:18990.
10. Nielsen L., Khurana R., Coats A., Frokjaer S., Brange J., Vyas S., Uversky V.N., Fink A.L. Biochemistry 2001, 40:6036.
11. Bouchard M., Zurdo J., Nettleton E.J., Dobson C.M., Robinson C.V. Protein Sci. 2000, 9:1960.
12. Mollmann S.H., Bukrinsky J.T., Frokjaer S., Elofsson U. J. Colloid Interface Sci. 2005, 286:28.
13. Nilsson P., Nylander T., Havelund S. J. Colloid Interface Sci. 1991, 144:145.
14. Buijs J., Vera C.C., Ayala E., Steensma E., Håkansson P., Oscarsson S. Anal. Chem. 1999, 71:3219.
15. Ballet T., Bruckert F., Mangiagalli P., Bureau C., Boulangé L., Nault L., Perret T., Weidenhaupt M. Biochemistry 2012, 51:2172.
16. Sluzky V., Klibanovt A.M., Langer R. Biotechnol. Bioeng. 1992, 40:895.
17. Kowalewski T., Holtzman D.M. Proc. Natl. Acad. Sci. U.S.A. 1999, 96:3688.
18. Zhu M., Souillac P.O., Ionescu-Zanetti C., Carter S.A., Fink A.L. J. Biol. Chem. 2002, 277:50914.
19. Pandey L.M., Pattanayek S.K. Appl. Surf. Sci. 2011, 257:4731.
20. Cassie A.B.D. Faraday Discuss. 1948, 3:11.
21. Kong J., Yu S. Acta Biochim. Biophys. Sin. 2007, 39:549.
22. Belyakova L.A., Varvarin A.M., Roik N.V. Appl. Surf. Sci. 2006, 253:784.
23. Tanford C., Epstein J. J. Am. Chem. Soc. 1954, 76:2163.
24. Giacomelli C.E., Norde W. Biomacromolecules 2003, 4:1719.