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Spider Silk and Amyloid Fibrils: A Structural Comparison
Author(s) -
Slotta Ute,
Hess Simone,
Spieß Kristina,
Stromer Thusnelda,
Serpell Louise,
Scheibel Thomas
Publication year - 2007
Publication title -
macromolecular bioscience
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.924
H-Index - 105
eISSN - 1616-5195
pISSN - 1616-5187
DOI - 10.1002/mabi.200600201
Subject(s) - spider silk , silk , spider , fibril , amyloid fibril , polymer science , amyloid (mycology) , chemistry , biophysics , materials science , amyloid β , biology , biochemistry , composite material , medicine , ecology , inorganic chemistry , disease , pathology
Although spider silks have been studied for decades, the assembly properties of the underlying silk proteins have still not been unravelled. Previously, the detection of amyloid‐like nanofibrils in the spider's silk gland suggested their involvement in the assembly process. Recombinantly produced spider silk also self‐assembles into nanofibrils. In order to investigate the structural properties of such silk nanofibrils in more detail, they have been compared to amyloid‐like fibrils to highlight structural similarities.