Abstract
Amphiphilic polypeptides, poly (γ-methyl L-glutamate) containing β-cyclodextrin as active end group (PMGn-CyD ; n=19, 24, 34) were prepared. The spectra of circular dichroism spectroscopy showed a-helical conformation of the PMG moiety. At the n-hexane/water interface, molecules of PMGn-CyD formed a stable monolayer. Interfacial pressure-area (π-A) isotherms suggested molecules of PMGn-CyD to be oriented almost normal to the n-hexane/water interface. When α-helical rods were oriented almost normal to the interface, 2-P-tolidilnyl-naphtalene-6-sulfonate (TNS) added as a guest molecule for CyD to the water phase under the monolayer caused fluctuation in interfacial pressure. Periodic movement of the PMGn-CyD monolayer due to the binding and release of guest molecules across the n-hexane/water interface was considered the reason for this.
