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Surface Characterization of As-Spun and Supercontracted Nephila clavipes Dragline Silk

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DOI: 10.4236/jsemat.2013.33A004    3,776 Downloads   5,582 Views   Citations


Dragline spider silks have relatively high mass-based mechanical properties (tensile strength, elongation to break and rupture energy) and are environmentally responsive (supercontraction). In order to produce new synthetic fibers with these properties, many research groups have focused on identifying the chemical composition of these fibers and the structure of the fiber core. Since each fiber also has an outer skin, our study will provide a detailed understanding of the silk surface morphology, the response of the surface morphology to environmental conditions and processing variables, and also determine if the silk surface has a definitive patterning of charged amino acids. Specifically, by using force microscopy and functionalized nanoparticles, the present study examines 1) how the silk surface (topography, average roughness) is altered due to prior mechanical loading (viz. reeling speed), 2) alterations in morphology due to environmental conditions (supercontraction, storage time), and 3) the negatively and positively charged regions along with the surface using both force and nanoparticle mapping. Roughness data taken on dragline silk collected from Nephila clavipes spiders revealed that the surface comprised both smooth (5 nm RMS) and rough (65 nm RMS) regions. Supercontracted silk (from immersion in0.01 MPBS during AFM testing) showed higher surface roughness values compared to spider silk tested in the air, indicating that the surface might be reorganized during supercontraction. No correlation was found between surface roughness and neither collection speed nor aging time for the as-spun or supercontracted fiber, demonstrating the surface stability of the dragline silk over time in terms of roughness. Both the force microscopy and the nanoparticle methods suggested that the density of negatively charged amino acids (glutamic acid, aspartic acid) was higher than that of the positively charged amino acids (lysine, asparagine, and histidine).

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The authors declare no conflicts of interest.

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B. Faugas, M. Ellison, D. Dean and M. Kennedy, "Surface Characterization of As-Spun and Supercontracted Nephila clavipes Dragline Silk," Journal of Surface Engineered Materials and Advanced Technology, Vol. 3 No. 3A, 2013, pp. 18-26. doi: 10.4236/jsemat.2013.33A004.


[1] F. Vollrath, “Strength and Structure of Spiders’ Silks,” Reviews in Molecular Biotechnology, Vol. 74, No. 2, 2000, pp. 67-83. doi:10.1016/S1389-0352(00)00006-4
[2] J. C. Zemlin, “A Study of the Mechanical Behavior of Spider’s Silks,” Technical Report 69-29-CM, AD 684333, US Army Natick Laboratories, Natick, 1968.
[3] R. W. Work, “The Force-Elongation Behavior of Web Fibers and Silks Forcibly Obtained from Orb-Web-Spinning Spider,” Textile Research Journal, Vol. 46, 1976, pp. 485-492.
[4] J. M. Gosline, P. A. Guerette, C. S. Ortlepp and K. N. Savage, “The Mechanical Design of Spider Silks: From Fibroin Sequence to Mechanical Function,” The Journal of Experimental Biology, Vol. 202, 1999, pp. 3295-3303.
[5] S. L. Stauffer, S. L. Coguill and R. V. Lewis, “Comparison of Physical Properties of three Silks from Nephila clavipes and Araneus Gemmoides,” The Journal of Arachnology, Vol. 22, No. 1, 1994, pp. 5-11.
[6] M. Hudspeth, X. Nie, W. N. Chen and R. V. Lewis, “Effect of Loading Rate on Mechanical Properties and Fracture Morphology of Spider Silk,” Biomacromolecules, Vol. 13, No. 8, 2012, pp. 2240-2246. doi:10.1021/bm3003732
[7] D. B. Zax, D. Armanios, S. Horak, C. Malowniak and Z. Yang, “Variation of Mechanical Properties with Amino Acid Content in the Silk of Nephila clavipes,” Biomacromolecules, Vol. 5, No. 3, 2004, pp. 732-738. doi:10.1021/bm034309x
[8] B. O. Swanson, T. A. Blackledge, J. Beltran and C. Y. Hayashi, “Variation in the Material Properties of Spider Dragline Silk Across Species,” Applied Physics A: Materials Science & Processing, Vol. 82, No. 2, 2006, pp. 213-218. doi:10.1007/s00339-005-3427-6
[9] P. M. Cunniff, S. A. Fossey, M. A. Auerbach, J. W. Song, D. Kaplan, W. W. Adams, R. K. Eby, D. Mahoney and D. L. Vezie, “Mechanical and Thermal Properties of Dragline Silk from the Spider Nephila clavipes,” Polymers for Advanced Technologies, Vol. 5, No. 8, 1994, pp. 401-410. doi:10.1002/pat.1994.220050801
[10] R. W. Work, “A Comparative Study of the Supercontraction of Major Ampullate Silk Fibers of Orb-Web-Building Spiders (Araneae),” Journal of Arachnology, Vol. 9, No. 3, 1981, pp. 299-308.
[11] L. W. Jelinski, A. Blye, O. Liivak, C. Michal, G. LaVerde, A. Seidel, N. Shah and Z. Yang, “Orientation, Structure, Wet-Spinning, and Molecular Basis for Supercontraction of Spider Dragline Silk,” International Journal of Biological Macromolecules, Vol. 24, No. 2-3, 1999, pp. 197-201. doi:10.1016/S0141-8130(98)00085-3
[12] T. A. Blackledge, C. Boutry, S. C. Wong, A. Baji, A. Dhinojwala, V. Sahni and I. Agnarsson, “How Super Is Supercontraction? Persistent versus Cyclic Responses to Humidity in Spider Dragline Silk,” Journal of Experimental Biology, Vol. 212, No. 13, 2009, pp. 1980-1988. doi:10.1242/jeb.028944
[13] K. N. Savage, P. A. Guerette and J. M. Gosline, “Supercontraction Stress in Spider Webs,” Biomacromolecules, Vol. 5, 2004, pp. 675-679. doi:10.1021/bm034270w
[14] I. Agnarsson, P. A. Guerette and J. M. Gosline, “Supercontraction Forces in Spider Dragline Silk Depend on Hydration Rate,” Zoology, Vol. 112, No. 5, 2009, pp. 325-331. doi:10.1016/j.zool.2008.11.003
[15] A. Sponner, W. Vater, S. Monajembashi, E. Unger, F. Grosse and K. Weisshart, “Composition and Hierarchical Organization of a Spider Silk,” PloS One, Vol. 2, No. 10, 2007, pp. 1-8. doi:10.1371/journal.pone.0000998
[16] K. Augsten, P. Mühlig and C. Herrmann, “Glycoproteins and Skin-Core Structure in Nephila clavipes Spider Silk Observed by Light and Electron Microscopy,” Scanning, Vol. 22, 2000, pp. 12-15. doi:10.1002/sca.4950220103
[17] L. Eisoldt, A. Smith and T. Schiebel, “Decoding the Secrets of Spider Silk,” Materials Today (Kidlington, England), Vol. 14, No. 3, 2011, pp. 80-86.
[18] M. Xu and R. V. Lewis, “Structure of a Protein Superfiber: Spider Dragline Silk,” Proceedings of the National Academy of Sciences, Vol. 87, No. 18, 1990, pp. 7120-7124. doi:10.1073/pnas.87.18.7120
[19] M. Hinman, J. Jones and R. V. Lewis, “Synthetic Spider Silk: A Modular Fiber,” Trends in Biotechnology, Vol. 18, No. 9, 2000, pp. 374-379. doi:10.1016/S0167-7799(00)01481-5
[20] J. O. Warwicker, “Comparative Studies of Fibroins: II. The Crystal Structures of Various Fibroins,” Journal of Molecular Biology, Vol. 2, 1960, pp. 350-362. doi:10.1016/S0022-2836(60)80046-0
[21] M. Creager, J. E. Jenkins, L. A. Thagard-Yeaman, A. E. Brooks, J. A. Jones, R. V. Lewis, G. P. Holland and J. L. Yarger, “Solid-State NMR Comparison of Various Spiders’ Dragline Silk Fiber,” Biomacromolecules, Vol. 11, No. 8, 2010, pp. 2039-2043. doi:10.1021/bm100399x
[22] J. D. Van Beek, S. Hess, F. Vollrath and B. H. Meier, “The Molecular Structure of Spider Dragline Silk: Folding and Orientation of the Protein Backbone,” PNAS: Proceedings of the National Academy of Sciences, Vol. 99, No. 16, 2002, pp. 10266-10271.
[23] R. H. Garrett and C. M. Grishman, “Biochemistry,” Brooks/Cole, 1999.
[24] B. Faugas, “Surface Characterization of Nephila clavipes Dragline Silk,” Master’s Thesis, Clemson University, Clemson, 2012.
[25] F. Vollrath, B. Madsen and Z. Shao, “The Effect of Spinning Conditions on the Mechanics of a Spider’s Dragline Silk,” Proceedings of the Royal Society B: Biological Sciences, Vol. 268, No. 1483, 2001, pp. 2339-2346. doi:10.1098/rspb.2001.1590
[26] P. J. Ramón-Torregrosa, M. A. Rodríguez-Valverdea, A. Amirfazlia and M. A. Cabrerizo-Vílcheza, “Factors Affecting the Measurement of Roughness Factor of Surfaces and its Implications for Wetting Studies,” Colloids and Surfaces A: Physicochemical and Engineering Aspects, Vol. 323, No. 1-3, 2008, pp. 83-93. doi:10.1016/j.colsurfa.2007.10.032
[27] J. Vandiver, D. Dean, N. Patel, W. Bonfield and C. Ortiz, “Nanoscale Variation in Surface Charge by Synthetic Hydroxyapatite Detected by Chemically and Spatially Specific High Resolution Force Spectroscopy,” Biomaterials, Vol. 25, No. 3, 2005, pp. 271-83. doi:10.1016/j.biomaterials.2004.02.053
[28] B. Zimmerman, J. Chow, A. G. Abbott, M. S. Ellison, M. S. Kennedy and D. Dean, “Variation of Surface Charge Along the Surface of Wool Fibers Assessed by High-Resolution Force Spectroscopy,” Journal of Engineered Fibers and Fabrics, Vol. 6, No. 2, 2011, pp. 61-66.
[29] B. Zimmerman, “Mechanical and Chemical Characterization of Biological Composite Structures,” Master’s Thesis, Clemson University, Clemson, 2009.
[30] G. T. Hermanson, “Bioconjugate Techniques,” Academic Press, Boston, 2008.
[31] N. Du, Z. Yang, X. Y. Liu, Y. Li and H. Y. Xu “Structural Origin of the Strain-Hardening of Spider Silk,” Advanced Functional Materials, Vol. 21, No. 4, 2011, pp. 772-778. doi:10.1002/adfm.201001397
[32] S. Lombardi and D. Kaplan, “The Amino Acid Composition of Major Ampullate Gland Silk (Dragline) of Nephila clavipes (Araneae, Tetragnathidae),” Journal of Arachnology, Vol. 18, No. 3, 1990, pp. 297-306.

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