Hostname: page-component-78c5997874-m6dg7 Total loading time: 0 Render date: 2024-11-05T01:40:25.119Z Has data issue: false hasContentIssue false
  • English
  • Français

Streptavidin-Phycoerythrin Conjugated Proteins Bound to Biotin on Langmuir-Blodgett Films of Biotinylated Lipid Monolayers

Published online by Cambridge University Press:  15 February 2011

Lynne A. Samuelson ,
D. L. Kaplan ,
K. A. Marx ,
P. Miller ,
D. M. Galotti ,
J. Kumar  and
S. K. Tripathy
Lynne A. Samuelson
Affiliation:
U.S. Army Natick Laboratories, Biotechnology Branch, Natick, MA 01760
D. L. Kaplan
Affiliation:
U.S. Army Natick Laboratories, Biotechnology Branch, Natick, MA 01760
K. A. Marx
Affiliation:
University of Lowell, Departments of Chemistry and Physics, Lowell, MA 01854
P. Miller
Affiliation:
University of Lowell, Departments of Chemistry and Physics, Lowell, MA 01854
D. M. Galotti
Affiliation:
University of Lowell, Departments of Chemistry and Physics, Lowell, MA 01854
J. Kumar
Affiliation:
University of Lowell, Departments of Chemistry and Physics, Lowell, MA 01854
S. K. Tripathy
Affiliation:
University of Lowell, Departments of Chemistry and Physics, Lowell, MA 01854
Get access

Abstract

Studies involving the specific and non-specific surface recognition of biotin on biotinylated LB lipid monolayers by streptavidin and avidin conjugated phycoerythrin are presented. Both streptavidin and avidin conjugates were injected under the monolayer and found to preferentially adsorb to the biotinylated monolayers at the air-water interface. Pressure-area isotherms displayed a biotin-streptavidin/avidin complex dependent increase in surface pressure at expanded areas indicating protein adsorption. The binding of protein was confirmed by transferring the monolayer films to solid supports and measuring the characteristic intense phycoerythrin fluorescence at 576 nm. The effect of protein charge, monolayer packing density and structure, and activation of the tetramer proteins towards specific and non-specific binding are discussed. These results suggest a novel and general methodology for the two-dimensional ordering of protein monolayers with potential bioelectronic, optical and protein structure research applications.

Type
Research Article
Information
MRS Online Proceedings Library (OPL) , Volume 218: Symposium V – Materials Synthesis Based on Biological Processes , 1990 , 159
Copyright
Copyright © Materials Research Society 1991

Access options

Get access to the full version of this content by using one of the access options below. (Log in options will check for institutional or personal access. Content may require purchase if you do not have access.)

References

REFERENCES

1. Kornberg, R.D. and Ribi, H.O., Protein Str., Folding and Design 2, 175 (1987).Google Scholar
2. Gantt, E., Bioscience 25 (12), 781 (1975).Google Scholar
3. Glazer, A.N., Ann. Rev. Biophys. Biophys. Chem. 14, 47 (1985).Google Scholar
4. Gantt, E., Ann. Rev. Plant Physiol. 32, 327 (1981).Google Scholar
5. Glazer, A.N. and Stryer, L., Trends in Biochemical Sciences October, 423 (1984).CrossRefGoogle Scholar
6. Holzwarth, A., Quarterly Reviews of Biophysics 22 (3) 239 (1989).CrossRefGoogle Scholar
7. Schirmer, T., Huber, R., Scheider, M., Bode, W., Miller, M., and Hackert, M.L., J. Molec. Biol. 188, 651 (1986).Google Scholar
8. Green, N.M., Adv. Protein Chem. 29, 85 (1975).CrossRefGoogle Scholar
9. Gimlick, R.K. and Giese, R.W., J. Biol. Chem. 263, 210 (1988).Google Scholar
10. Weber, P.C., Ohlendorf, P.C., Wendoloski, J.J., and Salemme, F.R., Science 243, 85 (1989).CrossRefGoogle Scholar
11. Gimlick, R.K. and Giese, R.W., J. Biol. Chem. 263, 210 (1988).Google Scholar
12. Blankenburg, R., Meller, P., Ringsdorf, H., and Salesse, C., Biochemistry 28, 8214 (1989).Google Scholar