title: Partially induced transition from horizontal to vertical orientation of helical peptides at the air-water interface and the structure of their monolayers transferred on the solid substrates.
abstract: To apply the Langmuir-Blodgett (LB) technique as a platform for investigating the fundamental properties of amphiphilic peptides (APs), we have investigated the structure of LB films 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, we are still far from having full control of their orientation. This study reports the contribution of the subphase temperature to the change in the orientation of helical APs. When the surface pressure-area isotherm of AP was observed at the subphase temperature at 41.5°C, the isotherm exhibited a plateau, implying that a phase transition of the monolayer at the air-water interface occurred. Circular dichroism (CD) spectra of the monolayers transferred on the solid substrates revealed that the orientation of the helices changed at the pressure, where the plateau of the isotherm was observed. This change was not observed at 21.5°C, i.e., the horizontal alignment of helixes was maintained. Atomic force microscopy (AFM) was used to systematically investigate the surface structure of the monolayers transferred at different surface pressures. A structural model of the monolayer that did not contradict with the results obtained by the three different techniques (the isotherm, CD spectroscopy, and AFM) was derived, and it was concluded that the horizontally oriented helices partially changed their orientation to vertical upon compression in the plateau region of the isotherm.
authors.affiliation: Graduate School of Science and Engineering, Meiji University, Kawasaki 214-8571, Japan; School of Science and Engineering, Meiji University, Kawasaki 214-8571, Japan. Electronic address: nkato@meiji.ac.jp.
authors.forename: Noritaka
authors.initials: N
authors.lastname: Kato
authors.affiliation: Graduate School of Science and Engineering, Meiji University, Kawasaki 214-8571, Japan; School of Interdisciplinary Mathematical Sciences, Meiji University, Tokyo 164-8525, Japan.
authors.forename: Takanori
authors.initials: T
authors.lastname: Sasaki
authors.affiliation: Graduate School of Science and Engineering, Meiji University, Kawasaki 214-8571, Japan; School of Science and Engineering, Meiji University, Kawasaki 214-8571, Japan.
authors.forename: Yuri
authors.initials: Y
authors.lastname: Mukai
mesh_terms: D000388:Air; D002462:Cell Membrane / Q000737:chemistry*; D002942:Circular Dichroism; D057927:Hydrophobic and Hydrophilic Interactions; D008567:Membranes, Artificial; D018625:Microscopy, Atomic Force; D008958:Models, Molecular; D010446:Peptide Fragments / Q000737:chemistry*; D044367:Phase Transition; D013499:Surface Properties; D013501:Surface-Active Agents / Q000737:chemistry*; D014867:Water / Q000737:chemistry*
chemical_list: D008567:Membranes, Artificial; D010446:Peptide Fragments; D013501:Surface-Active Agents; D014867:Water
keywords: Air–water interface; Amphiphilic peptide; Langmuir–Blodgett film; α-Helix