Construction of an arranged nano-fibrous structure by selforganization of a designed amphiphilic peptide based on β- strand

Abstract

AbstractAn amphiphilic peptide having alternate sequence of hydrophobic and charged amino acid residues, RFDF16 (CH3CO-RFDFRFDFRFDFRFDF-NH2), was designed to form a β-sheet monolayer at the air/water interface. The peptide monolayer was prepared by Langmuir-Blodgett (LB) method. The LB films were transferred onto mica substrates without the compressing process at various pH values in order to investigate a self-organized structure of peptide monolayer. Surface morphology of LB films showed arranged nano-fibers which have differences in interval between fibers and their orientation depending on pH of the subphase. On the other hand, the self-organized nano-fiber was also re-arranged by compressing process. The nano-fibers became elongated and aligned upon compression to higher surface pressures. The exploitation of an electrostatic interaction and compressing process will allow a larger two-dimensionally regulated nano-structure.