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PMID: 17295405 Published · ppublish English Comparative Study Journal Article Research Support, Non-U.S. Gov't

Spider silk and amyloid fibrils: a structural comparison.

Macromolecular bioscience ·Vol. 7 ·No. 2 ·2007-02-12 ·Pages 183-8

Slotta U, Hess S, Spiess K, Stromer T, Serpell L, Scheibel T

Abstract

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.

MeSH Terms
Amyloid/chemistry Animals Benzothiazoles Circular Dichroism Congo Red Fungal Proteins/chemistry Microscopy, Atomic Force Peptide Termination Factors Prions/chemistry Saccharomyces cerevisiae Proteins/chemistry Silk/chemistry Spectroscopy, Fourier Transform Infrared Spiders/chemistry Thiazoles/metabolism X-Ray Diffraction
Chemicals
Amyloid Benzothiazoles Fungal Proteins Peptide Termination Factors Prions SUP35 protein, S cerevisiae Saccharomyces cerevisiae Proteins Silk Thiazoles thioflavin T Congo Red
Authors & Affiliations
6 authors, click to expand affiliations / ORCID
Slotta Ute
Department Chemie, Lehrstuhl für Biotechnologie, Technische Universität München, Lichtenbergstr. 4, 85747 Garching, Germany.
Hess Simone
Spiess Kristina
Stromer Thusnelda
Serpell Louise
Scheibel Thomas
Article Info
Journal
Macromolecular bioscience
Abbr.
Macromol Biosci
ISSN
1616-5187
Published
2007-02-12
Pages
183-8
Language
English
Region
Germany
NLM ID
101135941
Subset
IM
Grants
Biotechnology and Biological Sciences Research Council · BB/A500061/1 · United Kingdom
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