Title :
Monolayer and atomic force microscopy studies of nicotinic acetylcholine receptor films
Author :
Palmer, Cynthia A. ; Fare, Thomas L. ; Turner, David C. ; Brandow, Susan L. ; Gaber, Bruce P. ; Silvestre, Cecile G. ; Cribbs, David H.
Author_Institution :
Naval Res. Lab., Washington, DC, USA
fDate :
Oct. 29 1992-Nov. 1 1992
Abstract :
The surface pressure-area and surface potential-area isotherms for the nicotinic acetylcholine receptor (nAChR) and several lipid-protein monolayers are reported. It was shown that buffer composition and pH affect the film isotherm; the addition of unsaturated lipid and cholesterol to the native protein film contributes to the fluid phase of the monolayer. Langmuir-Blodgett (LB) films of the lipid and lipid-protein monolayers transferred to silicon substrates were imaged using atomic force microscopy (AFM). The AFM images of lipid films show regular structure in the lipid layer and indicate protein aggregates in the AChR-lipid LB films, with feature sizes corresponding to the lipid and receptor molecular dimensions.
Keywords :
Langmuir-Blodgett films; aggregation; atomic force microscopy; lipid bilayers; molecular biophysics; monolayers; proteins; surface potential; thin films; AChR-lipid Langmuir-Blodgett films; AFM images; Si; atomic force microscopy; buffer composition; film isotherm; fluid phase; lipid layer; lipid-protein monolayers; nicotinic acetylcholine receptor films; protein aggregates; protein film; receptor molecular dimensions; regular structure; silicon substrate; surface potential-area isotherm; surface pressure-area isotherm; Atomic layer deposition; Lipidomics; Proteins;
Conference_Titel :
Engineering in Medicine and Biology Society, 1992 14th Annual International Conference of the IEEE
Conference_Location :
Paris
Print_ISBN :
0-7803-0785-2
Electronic_ISBN :
0-7803-0816-6
DOI :
10.1109/IEMBS.1992.5760885