Understanding self-assembled amphiphilic peptide supramolecular structures from primary structure helix propensity |
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Authors: | Baumann Martina K Textor Marcus Reimhult Erik |
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Institution: | Department of Materials Science, Laboratory for Surface Science and Technology (LSST), ETH Zurich, Zurich, Switzerland. |
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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. |
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