The role of salt and shear on the storage and assembly of spider silk proteins.
Major ampullate silk fibers of orb web-weaving spiders have impressive mechanical properties due to the fact that the underlying proteins partially fold into helical/amorphous structures, yielding relatively elastic matrices that are toughened by anisotropic nanoparticulate inclusions (formed from stacks of beta-sheets of the same proteins). In vivo the transition from soluble protein to solid fibers involves a combination of chemical and mechanical stimuli (such as ion exchange, extraction of water and shear forces). Here we elucidate the effects of such stimuli on the in vitro aggregation of engineered and recombinantly produced major ampullate silk-like proteins (focusing on structure-function relationships with respect to their primary structures), and discuss their relevance to the storage and assembly of spider silk proteins in vivo.
Eisoldt
Lukas
L
Fakultät für Angewandte Naturwissenschaften, Universität Bayreuth, Universitätsstr. 30, 95440 Bayreuth, Germany.
Hardy
John G
JG
Heim
Markus
M
Scheibel
Thomas R
TR
D000595:Amino Acid Sequence; D000818:Animals; D008422:Materials Testing; D008969:Molecular Sequence Data; D011487:Protein Conformation; D017510:Protein Folding; D011993:Recombinant Fusion Proteins / Q000737:chemistry / Q000235:genetics; D012492:Salts / Q000737:chemistry*; D033081:Shear Strength; D047011:Silk / Q000737:chemistry* / Q000235:genetics; D017550:Spectroscopy, Fourier Transform Infrared; D013112:Spiders / Q000033:anatomy & histology / Q000737:chemistry*; D013314:Stress, Mechanical
D011993:Recombinant Fusion Proteins; D012492:Salts; D047011:Silk