NR AVZX
AU Slotta,U.; Hess,S.; Spiess,K.; Stromer,T.; Serpell,L.; Scheibel,T.
TI Spider silk and amyloid fibrils: a structural comparison.
QU Macromolecular Bioscience 2007 Feb 12; 7(2): 183-8
PT comparative study; journal article; research support, non-u.s. gov't
AB 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.
MH Amyloid/*chemistry; Animals; Circular Dichroism; Congo Red; Fungal Proteins/*chemistry; Microscopy, Atomic Force; Prions/*chemistry; Silk/*chemistry; Spectroscopy, Fourier Transform Infrared; Spiders/*chemistry; Thiazoles/metabolism; X-Ray Diffraction
AD Department Chemie, Lehrstuhl für Biotechnologie, Technische Universität München, Lichtenbergstr. 4, 85747 Garching, Germany.
SP englisch
PO Deutschland