Morphological Modulation of Self-assembled Peptide by Aggregation-induced alpha-Helix/beta-Sheet Transition

摘要

Poly(ethylene glycol)(PEG)-appended peptide with a binary sequence of hydrophobic and hydrophilic amino acids with 16 residues gave grain-like aggregate in aqueous solution.The peptide segment in the aggregate adopted beta-sheet structure,while the peptide itself originally adopted alpha-helix structure.In the hydrophobic domain constructed by peptide segment,hydrogen bonding rearranged to give secondary structural transition.The alpha-helix/beta-sheet transition simultaneously gave morphological transition from a grain-like state to a fibrous object.