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• W1969809361 endingPage "2794" @default.
• W1969809361 startingPage "2789" @default.
• W1969809361 abstract "Abstract Fabrication of controlled peptide nanofibers with homogeneous morphology has been demonstrated. Amphiphilic β‐sheet peptides were designed as sequences of Pro‐Lys‐X 1 ‐Lys‐X 2 ‐X 2 ‐Glu‐X 1 ‐Glu‐Pro. X 1 and X 2 were hydrophobic residues selected from Phe, Ile, Val, or Tyr. The peptide FI (X 1 =Phe; X 2 =Ile) self‐assemble into straight fibers with 80–120 nm widths and clear edges, as examined by transmission electron microscopy (TEM) and atomic force microscopy (AFM). The fiber formation is performed in a hierarchical manner: β‐sheet peptides form a protofibril, the protofibrils assemble side‐by‐side to form a ribbon, and the ribbons then coil in a left‐handed fashion to make up a straight fiber. These type of fibers are formed from peptides possessing hydrophobic aromatic Phe residue(s). Furthermore, a peptide with Ala residues at both N and C termini does not form fibers (100 nm scale) with clear edges; this causes random aggregation of small pieces of fibers instead. Thus, the combination of unique amphiphilic sequences and terminal Pro residues determine the fiber morphology." @default.
• W1969809361 created "2016-06-24" @default.
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• W1969809361 date "2004-06-04" @default.
• W1969809361 modified "2023-10-17" @default.
• W1969809361 title "Fabrication of Nanofibers with Uniform Morphology by Self-Assembly of Designed Peptides" @default.
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• W1969809361 doi "https://doi.org/10.1002/chem.200305735" @default.
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