title: Silk Spinning in Silkworms and Spiders.
abstract: Spiders and silkworms spin silks that outcompete the toughness of all natural and manmade fibers. Herein, we compare and contrast the spinning of silk in silkworms and spiders, with the aim of identifying features that are important for fiber formation. Although spiders and silkworms are very distantly related, some features of spinning silk seem to be universal. Both spiders and silkworms produce large silk proteins that are highly repetitive and extremely soluble at high pH, likely due to the globular terminal domains that flank an intermediate repetitive region. The silk proteins are produced and stored at a very high concentration in glands, and then transported along a narrowing tube in which they change conformation in response primarily to a pH gradient generated by carbonic anhydrase and proton pumps, as well as to ions and shear forces. The silk proteins thereby convert from random coil and alpha helical soluble conformations to beta sheet fibers. We suggest that factors that need to be optimized for successful production of artificial silk proteins capable of forming tough fibers include protein solubility, pH sensitivity, and preservation of natively folded proteins throughout the purification and initial spinning processes.
authors: Department of Anatomy, Physiology and Biochemistry, Swedish University of Agricultural Sciences, Uppsala 75651, Sweden. marlene.andersson@slu.se.
authors: Marlene
authors: M
authors: Andersson
authors: Department of Anatomy, Physiology and Biochemistry, Swedish University of Agricultural Sciences, Uppsala 75651, Sweden. janne.johansson@ki.se.|Department of Neurobiology, Care Sciences and Society (NVS), Karolinska Institutet, Stockholm 14157, Sweden. janne.johansson@ki.se.
authors: Jan
authors: J
authors: Johansson
authors: Department of Anatomy, Physiology and Biochemistry, Swedish University of Agricultural Sciences, Uppsala 75651, Sweden. anna.rising@slu.se.|Department of Neurobiology, Care Sciences and Society (NVS), Karolinska Institutet, Stockholm 14157, Sweden. anna.rising@slu.se.
authors: Anna
authors: A
authors: Rising
mesh_terms: D000818:Animals; D012831:Bombyx / Q000378:metabolism*; D002256:Carbonic Anhydrases / Q000378:metabolism; D005349:Fibroins / Q000737:chemistry / Q000378:metabolism*; D011487:Protein Conformation; D047011:Silk / Q000737:chemistry* / Q000378:metabolism*; D013112:Spiders / Q000378:metabolism*
chemical_list: D047011:Silk; D005349:Fibroins; D002256:Carbonic Anhydrases
keywords: Bombyx mori; carbonic anhydrase; fibroin; major ampullate gland; pH gradient; protein conformation; spidroin