Abstract
The properties of gramicidin, a linear antibiotic polypeptide of 15 amino acids, have been studied at the air-water interface. Analysis of the pressure-area isotherm is not able to conclude about the conformational behavior of gramicidin in the monolayer. Langmuir-Blodgett deposition of gramicidin layers onto a mica substrate has been developed for atomic force microscopy (AFM) observations. At high pressure of deposition, the gramicidin monolayer is composed of dimers perpendicular to the surface. The possibility of removing the half upper part of this dimer monolayer with the AFM tip is more in favor of a structure of single-stranded helical dimers.