Premium
Fabrication of Nanofibers with Uniform Morphology by Self‐Assembly of Designed Peptides
Author(s) -
Matsumura Sachiko,
Uemura Shinobu,
Mihara Hisakazu
Publication year - 2004
Publication title -
chemistry – a european journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.687
H-Index - 242
eISSN - 1521-3765
pISSN - 0947-6539
DOI - 10.1002/chem.200305735
Subject(s) - nanofiber , peptide , amphiphile , random coil , transmission electron microscopy , fabrication , self assembly , fiber , morphology (biology) , materials science , crystallography , residue (chemistry) , ribbon , nanotechnology , chemistry , biophysics , polymer , copolymer , circular dichroism , biochemistry , composite material , medicine , alternative medicine , biology , genetics , pathology
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.