Interaction of actin-decorated liposomes with myosin molecules fixed on glass surface
Satoshi Iwabuchi, Kuniyuki Hatori
Department of Bio-system Engineering, Yamagata University
We prepared positively charged liposomes that consisted of dipalmitoylphoshatidylcholine and stearyl amine by either a hydration method or a spontaneous transfer method. When the mixture of the liposomes and actin filaments conjugated with rhodamine-phalloidin was observed under a fluorescent microscope, it was found that liposomes were decorated with actin filaments. The amount of actin filaments binding to the liposome was increased with an increase of content of stearyl amine in the liposome. The binding of actin filaments to the liposome surface was probably caused by electrostatic interaction. The actin-decorated liposomes could be bound to the heavy meromyosin molecules fixed on glass surface in the absence of ATP. Unfortunately, in the presence of ATP, actin-decorated liposomes could not move on heavy meromyosin molecules at present time. However, the amount of liposomes binding to myosin-coated surface was decreased by 45 % when ATP was added. This result showed that ATP-dependent dissociation of actin-decorated liposomes from myosin heads occurred.