Spider silk and amyloid fibrils: a structural comparison.
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.
Slotta
Ute
U
Department Chemie, Lehrstuhl für Biotechnologie, Technische Universität München, Lichtenbergstr. 4, 85747 Garching, Germany.
Hess
Simone
S
Spiess
Kristina
K
Stromer
Thusnelda
T
Serpell
Louise
L
Scheibel
Thomas
T
D000682:Amyloid / Q000737:chemistry*; D000818:Animals; D052160:Benzothiazoles; D002942:Circular Dichroism; D003224:Congo Red; D005656:Fungal Proteins / Q000737:chemistry*; D018625:Microscopy, Atomic Force; D010454:Peptide Termination Factors; D011328:Prions / Q000737:chemistry*; D029701:Saccharomyces cerevisiae Proteins / Q000737:chemistry*; D047011:Silk / Q000737:chemistry*; D017550:Spectroscopy, Fourier Transform Infrared; D013112:Spiders / Q000737:chemistry*; D013844:Thiazoles / Q000378:metabolism; D014961:X-Ray Diffraction
D000682:Amyloid; D052160:Benzothiazoles; D005656:Fungal Proteins; D010454:Peptide Termination Factors; D011328:Prions; C068068:SUP35 protein, S cerevisiae; D029701:Saccharomyces cerevisiae Proteins; D047011:Silk; D013844:Thiazoles; C009462:thioflavin T; D003224:Congo Red