A synthesized peptidolipid (C
18IIGLM-NH
2) comprised of a single C18-
saturated hydrocarbon chain connectedto the amino acid sequence IIGLM terminated with the NH
2 group was spread on water, which formed astable Langmuir monolayer. The Langmuir and Langmuir-Blodgett (LB) films have been characterized bymeasurements of surface pressure-area (
-A) and surface potential-area (
V-A) isotherms and infraredmultiple-angle
incidence resolution spectrometry (MAIRS). The Langmuir monolayer had a significantly largerlimiting molecular area than that of a similar molecule of C18IIGLM-OH, which was reported in our previousstudy. The surface dipole moment analysis coupled with the
-A isotherm suggested that the C
18IIGLM-NH
2 monolayer was extraordinarily stiff and the fundamental structure of the monolayer was brought aboutbefore the monolayer compression. The infrared MAIRS analysis of the C
18IIGLM-NH
2 LB film revealedthat the backbone structure of the monolayer was the 'antiparallel'
![](/images/gifchars/beta2.gif)
sheet aligned parallel to the substrate.Since the C
18IIGLM-OH LB film was made of 'parallel'
![](/images/gifchars/beta2.gif)
sheet with a random orientation, it has beenfound that the present C
18IIGLM-NH
2 Langmuir monolayer has a largely different monolayer structure,although the chemical structures are slightly different from each other by the terminal group only.