title: Understanding self-assembled amphiphilic peptide supramolecular structures from primary structure helix propensity.
abstract: Small amphiphilic peptides are attractive building blocks to design biocompatible supramolecular structures via self-assembly, with applications in, for example, drug delivery, tissue engineering, and nanotemplating. We address the influence of systematical changes in the amino acid sequence of such peptides on the self-assembled macromolecular structures. For cationic-head surfactant-like eight-residue peptides, the apolar tail amino acids were chosen to systematically vary the propensity to form an alpha-helical secondary structure while conserving the overall hydrophobicity of the sequence. Characterization of the supramolecular structures indicates that for short peptides a beta-sheet secondary structure correlates with ribbonlike assemblies while random-coil and alpha-helical secondary structures correlate with assembly of rods.
authors.affiliation: Department of Materials Science, Laboratory for Surface Science and Technology (LSST), ETH Zurich, Zurich, Switzerland.
authors.forename: Martina K
authors.initials: MK
authors.lastname: Baumann
authors.forename: Marcus
authors.initials: M
authors.lastname: Textor
authors.forename: Erik
authors.initials: E
authors.lastname: Reimhult
mesh_terms: D000595:Amino Acid Sequence; D002942:Circular Dichroism; D018625:Microscopy, Atomic Force; D046529:Microscopy, Electron, Transmission; D010455:Peptides / Q000737:chemistry*; D017433:Protein Structure, Secondary
chemical_list: D010455:Peptides