A synthesized peptidolipid (C18IIGLM-NH2) comprised of a single C18 saturated hydrocarbon chain connected to the amino acid sequence IIGLM terminated with the NH2 group was spread on water, which formed a stable Langmuir monolayer. The Langmuir and Langmuir-Blodgett (LB) films have been characterized by measurements of surface pressure area (pi-A) and surface potential area (ΔV-A) isotherms, and by infrared multiple-angle incidence resolution spectrometry (MAIRS). The Langmuir monolayer had a significantly larger limiting molecular area than that of a similar molecule of C18IIGLM-OH, which was reported in our previous study. The surface dipole moment analysis coupled with the pi-A isotherm suggested that the C18IIGLM-NH2 monolayer was extraordinarily stiff and the fundamental structure of the monolayer was brought about before the monolayer compression. The infrared MAIRS analysis of the C18IIGLM-NH2 LB film revealed that the backbone structure of the monolayer was the ‘anti-parallel’ beta-sheet aligned parallel to the substrate. Since the C18IIGLM-OH LB film was made of ‘parallel’ beta-sheet with a random orientation, it has been found that the present C18IIGLM-NH2 Langmuir monolayer has a largely different monolayer structure although the chemical structures are slightly different from each other by the terminal group only.
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