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Spider Silk and Amyloid Fibrils : A Structural Comparison

Title data

Slotta, Ute ; Hess, Simone ; Spieß, Kristina ; Stromer, Thusnelda ; Serpell, Louise ; Scheibel, Thomas:
Spider Silk and Amyloid Fibrils : A Structural Comparison.
In: Macromolecular Bioscience. Vol. 7 (February 2007) Issue 2 . - pp. 183-188.
ISSN 1616-5187
DOI: https://doi.org/10.1002/mabi.200600201

Abstract in another language

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.

Further data

Item Type: Article in a journal
Refereed: Yes
Keywords: ADF-4; FT-IR; Sup35p; X-ray; yeast prion
Institutions of the University: Faculties
Faculties > Faculty of Engineering Science
Faculties > Faculty of Engineering Science > Chair Biomaterials
Faculties > Faculty of Engineering Science > Chair Biomaterials > Chair Biomaterials - Univ.-Prof. Dr. Thomas Scheibel
Profile Fields > Advanced Fields > Advanced Materials
Profile Fields > Advanced Fields > Molecular Biosciences
Profile Fields > Advanced Fields > Polymer and Colloid Science
Profile Fields > Emerging Fields > Food and Health Sciences
Profile Fields
Profile Fields > Advanced Fields
Profile Fields > Emerging Fields
Result of work at the UBT: Yes
DDC Subjects: 600 Technology, medicine, applied sciences
600 Technology, medicine, applied sciences > 620 Engineering
Date Deposited: 25 Sep 2015 05:32
Last Modified: 20 May 2016 06:32
URI: https://eref.uni-bayreuth.de/id/eprint/19545