Abstract
An amphiphilic molecule that contains a tripeptide part forms an aggregate not only in water but also in nonpolar organic solvents. Fourie transform infrared (FT-IR) spectroscopy reveals that the aggregate in the organic solvents is a lyotropic liquid-crystal, because the alkyl chains within the aggregate in organic solvents are more disorderly than those within an aqueous aggregate which is the well-known lyotropic aggregate called the bilayer membrane. Although the aggregates contain a parallel β-sheet structure irrespective of the media, hydrogen bonding is more tightly formed in the nonpolar organic solvents. Therefore, the H-bonding prevents the alkyl chains from forming stable arrangements.
