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Fiber formation of a synthetic spider peptide derived from Nephila clavata
Author(s) -
Hidaka Yuji,
Kontani KoIchi,
Taniguchi Rina,
Saiki Masatoshi,
Yokoi Sayoko,
Yukuhiro Kenji,
Yamaguchi Hiroshi,
Miyazawa Mitsuhiro
Publication year - 2011
Publication title -
peptide science
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.556
H-Index - 125
eISSN - 1097-0282
pISSN - 0006-3525
DOI - 10.1002/bip.21402
Subject(s) - peptide , chemistry , spider , spider silk , circular dichroism , fiber , biopolymer , silk , combinatorial chemistry , peptide synthesis , biophysics , stereochemistry , biochemistry , organic chemistry , polymer , materials science , biology , ecology , composite material
Abstract Dragline silk is a high‐performance biopolymer with exceptional mechanical properties. Artificial spider dragline silk is currently prepared by a recombinant technique or chemical synthesis. However, the recombinant process is costly and large‐sized synthetic peptides are needed for fiber formation. In addition, the silk fibers that are produced are much weaker than a fiber derived from a native spider. In this study, a small peptide was chemically synthesized and examined for its ability to participate in fiber formation. A short synthetic peptide derived from Nephila clavata was prepared by a solid‐phase peptide method, based on a prediction using the hydrophobic parameter of each individual amino acid residue. After purification of the spider peptide, fiber formation was examined under several conditions. Fiber formation proceeded in the acidic pH range, and larger fibers were produced when organic solvents such as trifluoroethanol and acetonitrile were used at an acidic pH. Circular dichroism measurements of the spider peptide indicate that the peptide has a β‐sheet structure and that the formation of a β‐sheet structure is required for the spider peptide to undergo fiber formation. © 2010 Wiley Periodicals, Inc. Biopolymers (Pept Sci) 96: 222‐227, 2011.