Two-dimensional self-assembly of a designed amphiphilic peptide at air/water interface

Abstract

A peptide having alternate sequence of hydrophobic and hydrophitic amino acid residues. (QAQL)4 (CH3CO-(Gln-Ala-Gln- Leu) 4-NH2), was designed to form a β-sneet monolayer at the air-water interlace. According to the designing of the peptide having charge free amino acid as hydrophilic residues, the peptide showed stable monolayer at wide range pH. The peptide monolayer prepared by Lungmuir-Blodgen (LB) method showed an arranged nano-fibrous object (QAQL)4-PEG was also an attractive building block lor construction of nano-architecture by self-assembly at the air/water interface. PEG attached on the peptide segment showed a conformational transition from a flattened state to brush one, dependent on the compressing degree of the monolayer on water suhphase, The conformational transition was simultaneously induced a morphologieal change of the nano-architecture from disk-like structure to fibrous array. © 2008 The Society of Polymer Science, Japan.