Hostname: page-component-76fb5796d-9pm4c Total loading time: 0 Render date: 2024-04-25T12:19:53.709Z Has data issue: false hasContentIssue false
  • English
  • Français

Nanofiber Formation in Spider Dragline-Silk as Probed by Atomic Force Microscopy and Molecular Pulling

Published online by Cambridge University Press:  11 February 2011

Emin Oroudjev ,
Cheryl Y. Hayashi ,
Jason Soares ,
Steven Arcidiacono ,
Stephen A. Fossey  and
Helen G. Hansma
Emin Oroudjev
Affiliation:
Department of Physics, University of California, Santa Barbara, CA 93106, U.S.A.
Cheryl Y. Hayashi
Affiliation:
Department of Biology, University of California, Riverside, California 92521, U.S.A.
Jason Soares
Affiliation:
US Army Natick R&D Center, Natick, MA 01760, U.S.A.
Steven Arcidiacono
Affiliation:
US Army Natick R&D Center, Natick, MA 01760, U.S.A.
Stephen A. Fossey
Affiliation:
US Army Natick R&D Center, Natick, MA 01760, U.S.A.
Helen G. Hansma
Affiliation:
Department of Physics, University of California, Santa Barbara, CA 93106, U.S.A.
Get access

Abstract

Despite the extensive interest in its remarkable materials properties, the structure of spider dragline silk is not yet known. Indirect structural information is thus of particular interest. New data are presented here from two probe microscopy techniques – atomic force microscopy (AFM) and single-molecule force spectroscopy, or ‘molecular pulling.’ Using a soluble synthetic protein from dragline silk, segmented silk nanofibers have been observed by AFM. Molecular pulling (Force Spectroscopy) has revealed sawtooth-like rupture peaks, indicative of the sacrificial bonds and hidden lengths seen in molecules of other self-healing biomaterials. A model is presented for the folding of single dragline-silk molecules and the arrangement of these molecules into nanofibers. The relationship is discussed between these molecular / nanoscale results and the materials properties of natural and artificial dragline silks.

Type
Research Article
Information
MRS Online Proceedings Library (OPL) , Volume 738: Symposium G – Spatially Resolved Characterization of Local Phenomena in Materials and Nanostructures , 2002 , G10.4
Copyright
Copyright © Materials Research Society 2003

Access options

Get access to the full version of this content by using one of the access options below. (Log in options will check for institutional or personal access. Content may require purchase if you do not have access.)

References

REFERENCES

Oroudjev, E., Soares, J., Arcidiacono, S., Thompson, J. B., Fossey, S. A., and Hansma, H. G., “Segmented Nanofibers of Spider Dragline Silk: Atomic Force Microscopy and Single-Molecule Force Spectroscopy,” Proc. Natl. Acad. Sci. USA, vol. 99, pp. 6460–6465, 2002.Google Scholar
Service, R. F., “Mammalian Cells Spin a Spidery New Yarn,” Science, vol. 295, pp. 419b–421, 2002.Google Scholar
Lazaris, A., Arcidiacono, S., Huang, Y., Zhou, J.-F., Duguay, F., Chretien, N., Welsh, E. A., Soares, J. W., and Karatzas, C. N., “Spider Silk Fibers Spun from Soluble Recombinant Silk Produced in Mammalian Cells,” Science, vol. 295, pp. 472–476, 2002.Google Scholar
[4] Arcidiacono, S., Mello, C. M., Butler, M., Welsh, E., Soares, J. W., Allen, A., Ziegler, D., Laue, T., and Chase, S., “Aqueous processing and fiber spinning of recombinant spider silks,” Macromolecules, vol. 35, pp. 1262–1266, 2002.Google Scholar
[5] Prince, J. T., McGrath, K. P., Digiolamo, C. M., and Kaplan, D. L., “Construction, cloning, and expression of synthetic genes encoding spider dragline silk,” Biochemistry, vol. 34, pp. 10879–10885, 1995.Google Scholar
[6] Kindt, J. H., Sitko, J. C., Pietrasanta, L. I., Oroudjev, E., Becker, N., Viani, M. B., and Hansma, H. G., “Methods for Biological Probe Microscopy in Aqueous Fluids,” in Atomic Force Microscopy in Cell Biology, vol. 68, Methods in Cell Biology, Jena, B. P. and Hoerber, H., Eds. San Diego: Academic Press, 2002, pp. 213–230.Google Scholar
[7] Pietrasanta, L. I., Thrower, D., Hsieh, W., Rao, S., Stemmann, O., Lechner, J., Carbon, J., and Hansma, H. G., “Probing the Sacchromyces cervisiae CBF3-CEN DNA kinetochore complex using atomic force microscopy,” Proc. Natl. Acad. Sci. (USA), vol. 96, pp. 3757–3762, 1999.Google Scholar
[8] Schneider, S. W., Larmer, J., Henderson, R. M., and Oberleithner, H., “Molecular weights of individual proteins correlate with molecular volumes measured by atomic force microscopy,” Pflugers Arch, vol. 435, pp. 362–7, 1998.Google Scholar
[9] Bustamante, C., Marko, J. F., Siggia, E. D., and Smith, S., “Entropic Elasticity of Lambda-Phage DNA,” Science, vol. 265, pp. 1599–1600, 1994.Google Scholar
[10] Seidel, A., Liivak, O., Calve, S., Adaska, J., Ji, G. D., Yang, Z. T., Grubb, D., Zax, D. B., and Jelinski, L. W., “Regenerated spider silk: Processing, properties, and structure,” Macromolecules, vol. 33, pp. 775–780, 2000.Google Scholar
[11] Gosline, J. M., Guerette, P. A., Ortlepp, C. S., and Savage, K. N., “The Mechanical Design of Spider Silks: from Fibroin Sequence to Mechanical Function,” J. Exp. Biol., vol. 202, pp. 3295–3303, 1999.Google Scholar