Abstract:
The Langmuir monolayer of cholesterol at the air-water interface exhibits a condensed phase in which the cholesterol molecules are aligned normal to the water surface. We have transferred the monolayer from water surface to different substrates by Langmuir-Blodgett (LB) technique and have studied their assembly by atomic force microscope (AFM). Our studies reveal that the aggregation of cholesterol molecules on hydrophobic surfaces leads to interesting structures. The cholesterol molecules assemble into a uniform film, elongated domains and uniformly distributed torus-shaped domains (doughnuts) for one, two and four cycles of deposition, respectively. Beyond four cycles, the molecules adsorb and desorb by an equal amount resulting in no further deposition. The formation of uniformly distributed doughnuts can be attributed to the hydrophobic interaction and reorganization of the molecules due to successive adsorption and desorption during deposition cycles. Our studies on hydrophilic surfaces show that cholesterol cannot form more than one layer of deposition.