Understanding self-assembled amphiphilic peptide supramolecular structures from primary structure helix propensity.
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.
Baumann
Martina K
MK
Department of Materials Science, Laboratory for Surface Science and Technology (LSST), ETH Zurich, Zurich, Switzerland.
Textor
Marcus
M
Reimhult
Erik
E
D000595:Amino Acid Sequence; D002942:Circular Dichroism; D018625:Microscopy, Atomic Force; D046529:Microscopy, Electron, Transmission; D010455:Peptides / Q000737:chemistry*; D017433:Protein Structure, Secondary
D010455:Peptides