The Monomolecular Organization of a Photodynamic Protein System Through Specific Surface Recognition of Streptavidin to Biotinylated LB Films
Technical rept. no. 18, 1 Jun 1990-31 May 1991
LOWELL UNIV MA DEPT OF CHEMISTRY
Pagination or Media Count:
This paper focuses on a novel methodology for the two-dimensional ordering of a photodynamic protein system using the Langmuir-Blodgett LB technique. The specific versus non-specific surface recognition of biotin or biotinylated LB monolayers by streptavidin and avidin conjugated phycoerthrin was investigated. Both avidin and streptavidin conjugates, when injected under the biotinylated monolayer, were found to preferentially adsorb to the biotin while at the air-water interface. Pressure-area isotherms displayed a biotin- streptavidinavidin complex dependent increase in surface pressure at expanded areas indicating protein adsorption. Fluorescence measurements of transferred films confirmed the binding of phycoerythrin to the monolayers and provided evidence that the avidin conjugated system may bind by both specific and non- specific mechanisms, while the streptavidin systems bind through only a specific mechanism. The extension of this methodology to any biotin or avidin streptavidin derivatized protein system is expected to lead to the fabrication of ultrathin, ordered, protein molecular assemblies with potential bioelectronic, optical and protein structure research applications.
- Organic Chemistry
- Physical Chemistry