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Vol 44(2010) N 1 p. 150-157; O.O. Sokolova1*, V.G. Bogush2, L.I. Davydova2, S.V. Polevova1, S.A. Antonov1, T.V. Neretina3, D.V. Klinov3, V.G. Debabov2, M.P. Kirpichnikov1 The Formation of a Quaternary Structure by Recombinant Analogs of Spider Silk Proteins 1Biological Faculty, Moscow State University, Moscow, 1199922State Research Center GosNIIGenetika, Moscow, 117545 Russia 3Shemyakin-Ovchinnikov Institute of Bioorganic Chemistry, Russian Academy of Sciences, Moscow, 117997 Russia *sokolova@moldyn.org Received - 2009-02-20; Accepted - 2009-04-16 The morphology of the fibers formed by recombinant analogs of dragline spider silk proteins, spidroins 1 and 2, was studied. It has been shown that the extension of the initial fiber, the so-called as-spun fiber, leads to remodeling of the spongy matrix with the formation of microfibers, which is accompanied by a decrease in the fiber diameter. The breaking strength of the fiber depends not only on the primary structure of the constituent protein, but also on the way it was formed. Simulation of the assembly of microfibers and the fibers formed of them can clarify the natural spider web spinning and enhance the development of technology for producing biomaterials with unique properties. recombinant proteins, spidroins, scanning electron microscopy, transmission electron microscopy, microfibers |
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