Efficiency of blocking of non-specific interaction of different proteins by BSA adsorbed on hydrophobic and hydrophilic surfaces

Journal of Colloid and Interface Science

Volumn 341, Issue 1, 2010, Pages 136-142

  Jeyachandran, Y L ^a   Mielczarski, J A ^a   Mielczarski, E ^a   Rai, B ^a  

^a Faculté des Sciences et Technologies   (France)

Author keywords

Adsorption of proteins; Blocking efficiency; BSA; Quantification

Indexed keywords

BLOCKING EFFICIENCY; BOVINE SERUM ALBUMINS; BSA; BSA MOLECULES; CLOSE-PACKED MONOLAYERS; COMPETITIVE ADSORPTION; CONCANAVALIN A; HYDROPHILIC SURFACES; HYDROPHOBIC AND HYDROPHILIC; IMMUNOGLOBULIN G; INCUBATION TIME; INFRARED REFLECTION SPECTROSCOPY; NON-SPECIFIC INTERACTIONS; NONSPECIFIC ADSORPTION; OPTIMISATIONS; QUANTIFICATION; SOLUTION CONCENTRATION; SPECTRAL SIMULATIONS; STAPHYLOCOCCAL PROTEIN; SURFACE COMPLEX; SURFACE COVERAGES;

ADSORPTION; DESORPTION; DYES; HYDROPHILICITY; HYDROPHOBICITY; INFRARED SPECTROSCOPY; MONOLAYERS; PROTEINS;

BODY FLUIDS;

BOVINE SERUM ALBUMIN; CONCANAVALIN A; IMMUNOGLOBULIN G; PHOSPHATE; STAPHYLOCOCCUS PROTEIN A;

ADSORPTION KINETICS; ARTICLE; COMPETITIVE INHIBITION; COMPLEX FORMATION; CONCENTRATION (PARAMETERS); CONFORMATIONAL TRANSITION; CONTROLLED STUDY; DESORPTION; HYDROPHILICITY; HYDROPHOBICITY; INCUBATION TIME; INFRARED SPECTROSCOPY; PRIORITY JOURNAL; PROCESS OPTIMIZATION; PROTEIN ANALYSIS; PROTEIN PROTEIN INTERACTION; QUALITATIVE ANALYSIS; QUANTITATIVE ANALYSIS; SURFACE PROPERTY;

ADSORPTION; ANIMALS; CATTLE; HYDROPHOBICITY; PROTEINS; SERUM ALBUMIN, BOVINE; WATER;

EID: 70350619879     PISSN: 00219797     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.jcis.2009.09.007     Document Type: Article

References (40)

1. Shen M., and Horbett T.A. J. Biomed. Mater. Res. 57 (2001) 336-345
2. Nam J.M., Thaxton C.S., and Mirkin C.A. Science 301 (2003) 1884-1886
3. Sandu C., and Singh R.K. Food Technol. 45 (1991) 84-91
4. Costerton J.W., Cheng K.-J., Geesey G.G., Ladd T.I., Nickel J.C., Dasgupta M., and Marrie T. J. Annu. Rev. Microbiol. 41 (1987) 435-464
5. Rechnitz G.A. Chem. Eng. News 66 (1988) 24-36
6. Rankl M., Ruckstuhl T., Rabe M., Artus G.R.J., Walser A., and Seeger S. Chem. Phys. Chem. 7 (2006) 837-846
7. Ishihara K., Oshida H., Endo Y., Ueda T., Watanabe A., and Nakabayashi N. J. Biomed. Mater. Res. 26 (1992) 1543-1552
8. Brorson S.-H. Micron 28 (1997) 189-195
9. Steinitz M. Anal. Biochem. 282 (2000) 232-238
10. Reimhult K., Pertersson K., and Krozer A. Langmuir 24 (2008) 8695-8700
11. E.S. Sawyer, P.J. Sawyer, United States Patent 5602041, 1997.
12. Heller A. Micron 26 (1995) 15-24
13. Gibbs J. Effective Blocking Procedures: ELISA Technical Bulletin - No. 3 (2001), Corning Incorporation Life Sciences
14. Sweryda-Krawiec B., Deveraj H., Jacob G., and Hickman J.J. Langmuir 20 (2004) 2054-2056
15. Ramsden J.J., Bachmanova G.I., and Archakov A.I. Biosens. Bioelectron. 11 (1996) 523-528
16. Ramsden J.J., and Schneider P. Biochemistry 32 (1993) 523-529
17. Kurrat R., Ramsden J.J., and Prenosil J.E. J. Chem. Soc. Faraday Trans. 90 (1994) 587-590
18. Kurrat R., Prenosil J.E., and Ramsden J.J. J. Colloid Interface Sci. 185 (1997) 1-8
19. Fernandez A., and Ramsden J.J. J. Biol. Phys. Chem. 1 (2001) 81-84
20. Jeyachandran Y.L., Mielczarski E., Rai B., and Mielczarski J.A. Langmuir 9 July (2009) 10.1021/la901453a
21. Dancil K.-P.S., Greiner D.P., and Sailor M.J. J. Am. Chem. Soc. 121 (1999) 7925-7930
22. Tan L., Xie Q., and Yao S. Bioelectrochemisty 70 (2007) 348-355
23. Mielczarski J.A., Dong J., and Mielczarski E. J. Phys. Chem. B 112 (2008) 5228-5237
24. Dong J., Mielczarski J.A., Mielczarski E., and Xu Z. Biotechnol. Prog. 24 (2008) 972-980
25. Hansen W.N.J. J. Opt. Soc. Am. 58 (1968) 380-390
26. Noinville S.S., Revault M., Quiquampoix H., and Baron M.-H. J. Colloid Interface Sci. 221 (2000) 273-283
27. Murayama K., and Tomida M. Biochemistry 43 (2004) 11526-11532
28. Goormaghtigh E., Ruysschaert J.M., and Raussens V. Biol. J. 90 (2006) 2946-2957
29. Sugio S., Kashima A., Mochizuki S., Nioda M., and Kobayashi K. Protein Eng. 12 (1999) 439-446
30. Bouckaert J., Dewallef Y., Poortmans F., Wyns L., and Loris R. J. Biol. Chem. 275 (2000) 19778-19787
31. Sjodahl J. Eur. J. Biochem. 73 (1977) 343-351
32. Guss B., Uhlen M., Nilsson B., Lindberg M., Sjoquist J., and Sjodahl J. Eur. J. Biochem. 138 (1984) 413-420
33. Buijs J., and Norde W. Langmuir 12 (1996) 1605-1613
34. Perkins S.J., and Sim R.B. Eur. J. Biochem. 157 (1986) 155-168
35. Tronin A., Dubrovsky T., and Nicolini C. Langmuir 11 (1995) 385-389
36. Sjoholm I. Eur. J. Biochem. 51 (1975) 55-61
37. Kim J., and Somorjai G.A. J. Am. Chem. Soc. 125 (2003) 3150-3158
38. Norde W., and Giacomelli C.E. Macromol. Symp. 145 (1999) 125-136
39. Vermeer A.W.P., Giacomelli C.E., and Norde W. Biochim. Biophys. Acta 1526 (2001) 61-69
40. Fabian H., and Naumann D. Methods 34 (2004) 28-40