Abstract
A peptide having alternate sequence of hydrophobic and hydrophilic amino acid residues, (QAQL)4 (CH3CO-(Gln-Ala-Gln-Leu)4-NH2), was designed to form a β-sheet monolayer at the air/water interface. 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 Langmuir-Blodgett (LB) method showed an arranged nano-fibrous object. (QAQL)4-PEG was also an attractive building block for 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 subphase. The conformational transition was simultaneously induced a morphological change of the nano-architecture from disk-like structure to fibrous array.
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