Skip to main content Accessibility help
×
Home

Molecular Order in Silk Secretions

  • Christopher Viney (a1), Keven Kerkam (a2), Lisa Gilliland (a3), David Kaplan (a4) and Stephen Fossey (a4)...

Abstract

Transmitted polarized light microscopy of various natural silk secretions reveals their ability to form nematic liquid crystalline phases. Observations of microstructure, together with a simple secondary structure analysis of known amino acid sequences in silk proteins, suggest that the rodlike structures forming the nematic phase are supramolecular aggregates, rather than individual rigid molecular segments. The optical birefringence of dragline fiber produced by controlled silking depends on the linear haul-off velocity, and can exceed the birefringence of naturally spun fibers; this suggests the possibility of in-vitro spinning of silk to obtain values of strength and stiffness even greater than those achieved in vivo.

Copyright

References

Hide All
1. Gosline, J.M., DeMont, M.E. and Denny, M.W., Endeavour 10, 37 (1986).
2. Kaplan, D.L., Lombardi, S.J. et al. in Biomaterials: Novel Materials from Biological Sources, edited by Byrom, D. (Stockton Press, New York, 1991) p. 3.
3. Peakall, D.B., J. Exp. Zool. 176, 257 (1971).
4. Levi, H.W., Spiders and their Kin (Golden Press, New York, 1987).
5. Case, S.T., Wellman, S.E. and Hamodrakas, S. in Materials Synthesis Based On Biological Processes, edited by Alper, M. et al. (Mater. Res. Soc. Proc. 218, Pittsburgh, PA, 1991) pp. 233237.
6. Foelix, R.F., Biology of Spiders (Harvard University Press, Cambridge, MA, 1982) p.121.
7. Kerkam, K., Viney, C., Kaplan, D.L. and Lombardi, S.J., Nature 349, 596 (1991).
8. Kerkam, K., Kaplan, D.L. et al. in Materials Synthesis Based on Biological Processes, edited by Alper, M. et al. (Mater. Res. Soc. Proc. 218, Pittsburgh, PA, 1991) pp. 239244.
9. Gray, G.W. and Goodby, J.W.G., Smectic Liquid Crystals: Textures and Structures (Leonard Hill, Glasgow, 1984).
10. Papkov, S.P., Adv. in Polym. Sci. 59, 75 (1984).
11. Flory, P.J., Proc. Roy. Soc. Lond. A 234, 73 (1956).
12. Flory, P.J. and Ronca, G., Mol. Cryst. Liq. Cryst. 54, 289 (1979).
13. Tsujimoto, Y. and Suzuki, Y., Cell 18, 591 (1979).
14. Lucas, F. and Rudall, K.M. in Comprehensive Biochemistry: Extracellular and Supporting Structures, edited by Florkin, M. and Stotz, E.H. (Elsevier, Amsterdam, 1968) p. 475.
15. Strydom, D.J., Haylett, T. and Stead, R.H., Biochem. and Biophys. Res. Comm. 27, 932 (1977).
16. Rawn, J.D., Proteins. Energy. and Metabolism (Neil Patterson, Burlington, NC, 1989) p. 80.
17. Xu, M. and Lewis, R.V., Proc. Nat. Acad. Sci. USA 87, 7120 (1990).
18. Chou, P.Y. and Fasman, G.D., Ann. Rev. Biochem. 41,251 (1978).
19. Kyte, J. and Doolittle, R.F., J. Mol. Biol. 157, 105 (1982).
20. Asakura, T., Makromol. Chem., Rapid Comm. 7, 755 (1986).
21. Dannels, C.M., Viney, C. et al. , Mol. Cryst. Liq. Cryst. 198, 341 (1991).
22. Wilson, R.S., Quarterly Journal of Microscopic Science 104, 557 (1962).

Molecular Order in Silk Secretions

  • Christopher Viney (a1), Keven Kerkam (a2), Lisa Gilliland (a3), David Kaplan (a4) and Stephen Fossey (a4)...

Metrics

Full text views

Total number of HTML views: 0
Total number of PDF views: 0 *
Loading metrics...

Abstract views

Total abstract views: 0 *
Loading metrics...

* Views captured on Cambridge Core between <date>. This data will be updated every 24 hours.

Usage data cannot currently be displayed