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Biosynthesis and Processing of Silk Proteins

Published online by Cambridge University Press:  29 November 2013

David L. Kaplan ,
Stephen Fossey ,
Charlene M. Mello ,
Steven Arcidiacono ,
Kris Senecal ,
Wayne Muller ,
Scott Stockwell ,
Richard Beckwitt ,
Christopher Viney  and
Keven Kerkam
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Extract

Silks produced by silkworms (e.g., Bombyx mori) and orb-web weaving spiders (e.g., Nephila clavipes) are essentially pure protein, that is, complexes of amino acid polymers. They are the most common fibers spun by biological systems. There has been a long-standing interest in the use of these and similar fibers in textiles, cables, fiber reinforcement in composites, in addition, for example, to cross hairs in optical instruments, and fishing nets. Both nylon, a homo-polymer of the amino acid glycine, and Kevlar, a polymer of a nonnatural aromatic amino acid, can be considered modified, synthetic versions of silk and are used for some of the applications mentioned above. The potential for genetic manipulation, through recombinant DNA technology, of the natural biosynthetic process for these natural proteins (see the article by Cappello in this issue) has renewed interest in the production of new silklike proteins.

The natural silks are characterized by a β-sheet secondary structure which is stabilized by interchain hydrogen bonds and intersheet hydrophobic interactions (Figure 1). Silks can be considered block copolymers, with crystalline domains consisting of short side chain monomers (the amino acids glycine, alanine, and serine) interspersed in amorphous domains consisting of bulkier side chain amino acids.

This family of fibers is naturally tailored to perform functions such as catching prey (orb web) or serving as a barrier against environmental challenges (cocoon). The domestic silkworm (B. mori) produces only one type of silk, cocoon silk, at only one stage in its lifecyle, during the fifth larval instar just before molt to the pupa. The silk is produced in modified salivary glands and spun from the mouth.

Type
Biology and Materials Synthesis
Information
MRS Bulletin , Volume 17 , Issue 10 , October 1992 , pp. 41 - 47
Copyright
Copyright © Materials Research Society 1992

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References

1.Kaplan, D.L., Lombardi, S.J., Muller, W.S. and Fossey, S.A., in Biomaterials: Novel Materials from Biological Sources, edited by Byrom, D. (Stockton Press, New York, 1991) Chapter I.Google Scholar
2.Lombardi, S.J., Fossey, S. and Kaplan, D.L., in Proc. Am. Soc.for Composites, Fifth Techn. Conf. (Technomic Pub. Co., Lancaster, PA, 1990) p. 184–187.Google Scholar
3.Gage, L.P. and Manning, R.F., J. Biol. Chem. 255 (1980) p. 9444.CrossRefGoogle Scholar
4.Gage, L.P. and Manning, R.F., J. Biol. Chem. 255 (1980) p. 9451.CrossRefGoogle Scholar
5.Kaplan, D.L., Fossey, S.A., Viney, C., and Muller, W.S., in Hierarchically Structured Materials, edited by Aksay, I.A., Baer, Eric, Sarikaya, M., and Tirrell, D. (Mater. Res. Soc. Symp. Proc. 255, Pittsburgh, PA, 1992) p. 19–30.Google Scholar
6.Hong, S.Y. and Kertesz, M., Phys. Rev. B. 41 (1990) p. 11368.CrossRefGoogle Scholar
7.Liable, R., Ballistic Materials and Penetration Mechanics (Elsevier, New York, 1980).Google Scholar
8.Work, R., J. Exp. Biol. 118 (1985) p. 379.CrossRefGoogle Scholar
9.Zemlin, J.C., Report 69-29-CM (AD684333), U.S. Army Natick Laboratories, Natick, Massachusetts (1968).Google Scholar
10.Gosline, J.M., DeMont, M.E., and Denny, M.W., Endeavour 10 (1986) p. 37.CrossRefGoogle Scholar
11.Gosline, J.M., Denny, M.W., and DeMont, M.E., Nature 309 (1984) p. 551.CrossRefGoogle Scholar
12.Young, L.S., Takahashi, N., and Sprague, K.U., Proc. Natl. Acad. Sci. 83 (1986) p. 374.CrossRefGoogle Scholar
13.Lombardi, S.J. and Kaplan, D.L., Arachnol. 18 (1990) p. 297.Google Scholar
14.Lucas, F., Shaw, J.T.B., and Smith, S.G., Adv. Prot. Chem. 13 (1958) p. 107.Google Scholar
15.Stydom, D.J., Haylett, T., and Stead, R.H., Biochem. Biophys. Res. Commun. 79 (1977) p. 932.CrossRefGoogle Scholar
16.Xu, M., Lewis, R.V., Proc. Nat. Acad. Sci. 87 (1990) p. 7120.CrossRefGoogle Scholar
17.Oshima, Y. and Suzuki, Y., Proc. Natl. Acad. Sci. 74 (1977) p. 5363.CrossRefGoogle Scholar
18.Suzuki, Y. and Oshima, Y., Cold Spring Harbor Symp. Quant. Biol. 42 (1977) p. 147.Google Scholar
19.Lombardi, S.J. and Kaplan, D.L., Acta Zool. Fennica 190 (1991) p. 243Google Scholar
20.Lombardi, S.J. and Kaplan, D.L., Polymer Preprints, Div. Poly. Chem. Am. Chem. Soc. 31 (1990) p. 195.Google Scholar
21.Tsujimoto, Y. and Suzuki, Y., Cell 16 (1979), p. 425.CrossRefGoogle Scholar
22.Tsujimoto, Y. and Suzuki, Y., Cell 18 (1979) p. 591.CrossRefGoogle Scholar
23.Viney, C., Kerkam, K., Gilliland, L., Kaplan, D.L., and Fossey, S.A., in Complex Fluids, (Proceedings Materials Research Society, Pittsburgh, PA, 1992) in press.Google Scholar
24. Unpublished data.Google Scholar
25.Sibanda, T. and Thornton, J.M., Nature 316 (1985) p. 170.CrossRefGoogle Scholar
26.Fossey, S.A., Nemethy, G., Gibson, K.D., and Scheraga, H.A., Biopolym. 31 (1991) p. 1529.CrossRefGoogle Scholar
27.Tillinghast, E.K., Chase, S.F., and Townley, M.A., J. Insect Physiol. 30 (1984) p. 591.CrossRefGoogle Scholar
28.Kerkam, K., Viney, C., Kaplan, D.L., and Lombardi, S.J., Nature 349 (1991) p. 596.CrossRefGoogle Scholar
29.Case, S., Chromosoma 94 (1986) p. 483.CrossRefGoogle Scholar
30. Manuscript in preparation.Google Scholar
31.Demura, M., Asakura, T., Nakamura, E., and Tamura, H., J. Biotechnol. 10 (1989) p. 113.CrossRefGoogle Scholar