[17a-F206-1~12] 12.6 Nanobiotechnology

[17a-F206-11] Surface pressure-induced beta-alpha transition of amphiphilic peptides in a lipid monolayer at the air-water interface

Haruki Kato¹, Kentaro Kishida¹, 〇Noritaka Kato¹ (1.Meiji Univ.)

Keywords:amphiphilic peptides, secondary structure, Langmuir monolayers

To apply the Langmuir monolayer technique as a platform for investigating the fundamental properties of amphiphilic peptides (APs), we have investigated the structure of the monolayer using the APs. To vertically orient the helical APs like transmembrane proteins in the membrane, the primary structure of the APs was designed to have two domains: a hydrophilic domain (three amino acids) and a hydrophobic domain (ca. 20 amino acids). However, full controls of their orientation and conformation are hardly realized. We report the alpha-beta transition of the newly-designed AP in the lipid monolayer at the air-water interface. This transition was reversible. The miscibility between the AP and lipids and the film structure will be also discussed.