蚕丝和蜘蛛丝纤维：从溶解性蛋白到超级纤维.pptVIP

Deduced amino acid sequence of B. mori H-fibroin. The representative sequence (between residues 1619 to 2642) is arranged to reveal characteristic repeat motifs that make up three highest order repeat assemblies. Residues Tyr and Val that disturb regularity are printed in bold and underlined, and the repeat termini (typically GAAS) are double underlined. Noncrystalline (amorphous) spacers are shown in italics. In B. mori, a string of GAGAGS motifs occupies most of the repeat length, but close to the repeat end, it is interrupted by a Tyr-rich sequence that is mostly 21 residues long. Uneven GAGAGS motifs are shadowed to accentuate regularity of their repetitions. α-Chymotrypsin cleaves B. mori silk selectively in the amorphous “linker” regions of the protein, allowing the crystalline regions to self-assemble into larger structures than would be possible in the native form. * Wide angle X-ray scattering pattern from a bundle of B. mori silk fibers with the long axes of the fibers oriented vertically. * In terms of manipulation, Shao and Vollrath have shown that, by changing the reeling conditions, silkworm silks can be made stronger, stiffer and more extensible, approaching the properties of spider dragline silk. * Spider dragline silk proteins are stored in the ampulla of the major ampullate gland until they are processed into fibers. During the natural spinning process, the proteins move distally through the gland, where they encounter changes in their biochemical environment and elongational and shear forces. This pH drop, along with altered salt concentration, dehydration, and shear forces, is involved in the assembly of soluble spidroins into fibrils. * There are also experiments in vivo to investigate the silk fiber formation from silkworms, showing that reeling silk fibers from live silkworms and spiders at a high speed (e g, 400 mm·s－1) have better mechanical properties. These proteins are synthesized in specialized sets of modified salivary glands befo