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“Biosteel”: an exciting product from nature that is superior to many manmade alternatives

  • Soumyadip Majumder

    Soumyadip Majumder is currently a PhD student at the Department of Chemical and Biomolecular Engineering, Hong Kong University of Science and Technology (HKUST). He obtained his Bachelor’s degree in Chemical Engineering from the National Institute of Technology, Durgapur, India, in 2011 and received his Master’s degree in Chemical Engineering from the Indian Institute of Technology, Kharagpur, India, in 2014. His current research area focuses on the development of advanced materials for lithium sulfur batteries. Previously, he also worked on the antimicrobial coating of cupric oxide nanoparticles on medical fabrics.

    , Mahadev D. Kaulaskar

    Mahadev D. Kaulaskar completed his Master’s in Chemical Engineering from the Indian Institute of Technology, Kharagpur, India, in 2006.

    and Sudarsan Neogi

    Sudarsan Neogi is currently a Professor in the Department of Chemical Engineering, I.I.T. Kharagpur. He obtained his Bachelor’s and Master’s in Chemical Engineering from the University of Calcutta, India. He obtained his PhD from the Ohio State University, USA. He has 12 years of industrial experience at Alcatel-Lucent. His research is focused mainly on the surface modification and engineering of polymer substrates by cold plasma for biomedical applications. He is also working on the treatment of wastewater by plasma.

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Published/Copyright: May 15, 2015
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Abstract

Biotechnology continues to offer routes for many exciting and unique products. Researchers genetically altered goats with a spider gene. These goats produce milk that contains a protein that can be extracted to produce biosteel fibers for use in bulletproof vests. It is referred to as “biosteel” to highlight its strength comparable to steel. This review paper describes the important aspects of produced dragline spider silk proteins via cell culture techniques using silk genes derived from two species of weaving spiders. These fibers were tested for a number of mechanical properties and compared to natural spider silk. In effect, fibers of biosteel were able to absorb similar amounts of energy as natural spider silk by stretching further. As opposed to most other synthetic fibers, biosteel is ecofriendly both in terms of its composition and production process.


Corresponding author: Sudarsan Neogi, Indian Institute of Technology, Department of Chemical Engineering, Kharagpur 721302, West Bengal, India, e-mail:

About the authors

Soumyadip Majumder

Soumyadip Majumder is currently a PhD student at the Department of Chemical and Biomolecular Engineering, Hong Kong University of Science and Technology (HKUST). He obtained his Bachelor’s degree in Chemical Engineering from the National Institute of Technology, Durgapur, India, in 2011 and received his Master’s degree in Chemical Engineering from the Indian Institute of Technology, Kharagpur, India, in 2014. His current research area focuses on the development of advanced materials for lithium sulfur batteries. Previously, he also worked on the antimicrobial coating of cupric oxide nanoparticles on medical fabrics.

Mahadev D. Kaulaskar

Mahadev D. Kaulaskar completed his Master’s in Chemical Engineering from the Indian Institute of Technology, Kharagpur, India, in 2006.

Sudarsan Neogi

Sudarsan Neogi is currently a Professor in the Department of Chemical Engineering, I.I.T. Kharagpur. He obtained his Bachelor’s and Master’s in Chemical Engineering from the University of Calcutta, India. He obtained his PhD from the Ohio State University, USA. He has 12 years of industrial experience at Alcatel-Lucent. His research is focused mainly on the surface modification and engineering of polymer substrates by cold plasma for biomedical applications. He is also working on the treatment of wastewater by plasma.

References

Arcidiacono S, Mello C, Kaplan D, Cheley S, Bayley H. Purification and characterization of recombinant spider silk expressed in Escherichia coli. Appl Microbiol Biotechnol 1998; 49: 31–38.10.1007/s002530051133Search in Google Scholar PubMed

Arcidiacono S, Mello CM, Butler M, Welsh E, Soares JW, Allen A, Ziegler D, Laue T, Chase S. Aqueous processing and fiber spinning of recombinant spider silks. Macromolecules 2002; 35: 1262–1266.10.1021/ma011471oSearch in Google Scholar

Asakura T, Yao J, Yamane T, Umemura K, Ulrich AS. Heterogeneous structure of silk fibers from Bombyx mori resolved by 13C solid-state NMR spectroscopy. J Am Chem Soc 2002; 124: 8794–8795.10.1021/ja020244eSearch in Google Scholar PubMed

Bini E, Foo CW, Huang J, Karageorgiou V, Kitchel B, Kaplan DL. RGD functionalized bioengineered spider dragline silk biomaterial. Biomacromolecules 2006; 7: 3139–3145.10.1021/bm0607877Search in Google Scholar PubMed

Blackledge TA, Hayashi CY. Unraveling the mechanical properties of composite silk threads spun by cribellate orb-weaving spiders. J Exp Biol 2006; 209: 3131–3140.10.1242/jeb.02327Search in Google Scholar PubMed

Brooks AE, Stricker SM, Joshi SB, Kamerzell TJ, Middaugh CR, Lewis RV. Properties of synthetic spider silk fibers based on Argiope aurantia MaSp2. Biomacromolecules 2008; 9: 1506–1510.10.1021/bm701124pSearch in Google Scholar PubMed

Cai K, Hu Y, Jandt KD. Surface engineering of titanium thin films with silk fibroin via layer-by-layer technique and its effects on osteoblast growth behavior. J Biomed Mater Res 2007; 82: 927–935.10.1002/jbm.a.31233Search in Google Scholar PubMed

Cassinelli C, Cascardo G, Morra M, Draghi L, Motta A, Catapano G. Physical-chemical and biological characterization of silk fibroin-coated porous membranes for medical applications. Int J Artif Organs 2006; 29: 881–892.Search in Google Scholar

Chung H, Kim TY, Lee SY. Recent advances in production of recombinant spider silk proteins. Curr Opin Biotechnol 2012; 23: 957–964.10.1016/j.copbio.2012.03.013Search in Google Scholar PubMed

Fahnestock SR, Bedzyk LA. Production of synthetic spider dragline silk protein in Pichia pastoris. Appl Microbiol Biotechnol 1997; 47: 33–39.10.1007/s002530050884Search in Google Scholar PubMed

Fahnestock SR, Irwin SL. Synthetic spider dragline silk proteins and their production in Escherichia coli. Appl Microbiol Biotechnol 1997; 47: 23–32.10.1007/s002530050883Search in Google Scholar PubMed

Freiberg S, Zhu XX. Polymer microspheres for controlled drug release. Int J Pharm 2004; 282: 1–18.10.1016/j.ijpharm.2004.04.013Search in Google Scholar

Gatesy J, Hayashi C, Motriuk D, Woods J, Lewis R. Extreme diversity, conservation, and convergence of spider silk fibroin sequences. Science 2001; 291: 2603–2605.10.1126/science.1057561Search in Google Scholar

Gordon JE. Structures. United Kingdom: Penguin Books, 1978: 395.Search in Google Scholar

Gordon JE. The science of structures and materials. New York, NY: W.H. Freeman, 1988: 217.Search in Google Scholar

Gosline JM, Denny MW, DeMont ME. Spider silk as rubber. Nature 1984; 309: 551–552.10.1038/309551a0Search in Google Scholar

Gosline JM, DeMont ME, Denny MW. The structure and properties of spider silk. Endeavor 1986; 10: 37–43.10.1016/0160-9327(86)90049-9Search in Google Scholar

Gosline JM, Guerette PA, Ortlepp CS, Savage KN. The mechanical design of spider silks: from fibroin sequence to mechanical function. J Exp Biol 1999; 202: 3295–3303.10.1242/jeb.202.23.3295Search in Google Scholar

Gould P. Exploiting spider’s silk. Mater Today 2002; 5: 42–47.10.1016/S1369-7021(02)01238-5Search in Google Scholar

Grubb DT, Gending J. Molecular chain orientation in supercontracted and re-extended spider silk. Int J Biol Macromol 1999; 24: 203–210.10.1016/S0141-8130(98)00086-5Search in Google Scholar

Guinea GV, Elices M, Pérez-Rigueiro J, Plaza GR. Stretching of supercontracted fibers: a link between spinning and the variability of spider silk. J Exp Biol 2004; 208: 25–30.10.1242/jeb.01344Search in Google Scholar PubMed

Hardy JG, Römer LM, Scheibel TR. Polymeric materials based on silk proteins. Polymer 2008; 49: 4309–4327.10.1016/j.polymer.2008.08.006Search in Google Scholar

Hawthorn AC, Opell BD. Van der Waals and hygroscopic forces of adhesion generated by spider capture threads. J Exp Biol 2003; 206: 3905–3911.10.1242/jeb.00618Search in Google Scholar PubMed

Hayashi CY, Lewis R. Evidence from flagelliform silk cDNA for the structural basis of elasticity and modular nature of spider silks. J Mol Biol 1998; 275: 773–784.10.1006/jmbi.1997.1478Search in Google Scholar

Hayashi CY, Lewis RV. Molecular architecture controls the evolution of a modular spider silk protein gene. Science 2000; 287: 1477–1479.10.1126/science.287.5457.1477Search in Google Scholar

Hayashi CY, Lewis RV. Spider flagelliform silk: lessons in protein design, gene structure, and molecular evolution. Bioessays 2001; 23: 750–756.10.1002/bies.1105Search in Google Scholar

Hayashi CY, Shipley NH, Lewis RV. Hypotheses that correlate the sequence, structure, and mechanical properties of spider silk proteins. Int J Biol Macromol 1999; 24: 271–275.10.1016/S0141-8130(98)00089-0Search in Google Scholar

Hinman MB, Lewis RV. Isolation of a clone encoding a second dragline silk fibroin: Nephila clavipes dragline silk is a two protein fiber. J Biol Chem 1992; 267: 19320–19324.10.1016/S0021-9258(18)41777-2Search in Google Scholar

Hinman MB, Jones JA, Lewis RV. Synthetic spider silk: a modular fiber. Trends Biotechnol 2000; 18: 374–379.10.1016/S0167-7799(00)01481-5Search in Google Scholar

Hu X, Yuan J, Wang X, Vasanthavada K, Falick AM, Jones PR, La Mattina C, Vierra CA. Analysis of aqueous glue coating proteins on the silk fibers of the cob weaver: Latrodectus hesperus. Biochemistry 2007; 46: 3294–3303.10.1021/bi602507eSearch in Google Scholar PubMed

Huemmerich D, Helsen CW, Quedzuweit S, Oschmann J, Rudolph R, Scheibel T. Primary Structure elements of spider dragline silks and their contribution to protein solubility. Biochemistry 2004; 43: 13604–13612.10.1021/bi048983qSearch in Google Scholar PubMed

Ittah S, Michaeli A, Goldblum A, Gat U. A model for the structure of the C-terminal domain of dragline spider silk and the role of its conserved cysteine. Biomacromolecules 2007; 8: 2768–2773.10.1021/bm7004559Search in Google Scholar PubMed

Jackson GS, Hosszu LLP, Power A, Hill AF, Kenney J, Saibil H, Craven CJ, Waltho JP, Clarke AR, Collinge J. Reversible conversion of monomeric human prion protein between native and fibrilogenic conformations. Science 1999; 283: 1935–1937.10.1126/science.283.5409.1935Search in Google Scholar PubMed

Jelinski LW, Blye A, Liivak O, Michal C, LaVerde G, Seidel A, Shah N, Yang Z. Orientation, structure, wet-spinning and molecular basis for supercontraction of spider dragline silk. Int J Biol Macromol 1999; 24: 197–201.10.1016/S0141-8130(98)00085-3Search in Google Scholar

Jin HJ, Kaplan DL. Mechanisms of silk processing in insects and spiders. Nature 2003; 424: 1057–106.10.1038/nature01809Search in Google Scholar

Kerkam K, Viney C, Kaplan D, Lombardi S. Liquid crystallinity of natural silk secretions. Nature 1991; 424: 596–598.10.1038/349596a0Search in Google Scholar

Knight DP, Knight MM, Vollrath F. Beta transition and stress-induced phase separation in the spinning of spider dragline silk. Int J Biol Macromol 2000; 27: 205–210.10.1016/S0141-8130(00)00124-0Search in Google Scholar

Ko FK, Jovicic J. Modeling of mechanical properties and structural design of spider web. Biomacromolecules 2004; 5: 780–785.10.1021/bm0345099Search in Google Scholar

Kubik S. High Performance fibers from spider silk [in English]. Angew Chem Int Ed 2002; 41: 2721–2723.10.1002/1521-3773(20020802)41:15<2721::AID-ANIE2721>3.0.CO;2-3Search in Google Scholar

Langer R, Peppas NA. Advances in biomaterials, drug delivery, and bionanotechnology. AIChE J 2003; 49: 2990–3006.10.1002/aic.690491202Search in Google Scholar

Lawrence BD, Cronin-Golomb M, Georgakoudi I, Kaplan DL, Omenetto FG. Bioactive silk protein biomaterial systems for optical devices. Biomacromolecules 2008; 9: 1214–1220.10.1021/bm701235fSearch in Google Scholar

Lazaris A, Arcidiacono S, Huang Y, Zhou JF, Duguay F, Chretien N, Welsh EA, Soares JW, Karatzas CN. Spider silk fibers spun from soluble recombinant silk produced in mammalian cells. Science 2002; 295: 472–476.10.1126/science.1065780Search in Google Scholar

Li A, Zhou P, Shao Z, Xie X, Chen X, Wang H, Chunyu L, Yu T. The natural silk spinning process. Eur J Biochem 2001; 268: 6600–6606.10.1046/j.0014-2956.2001.02614.xSearch in Google Scholar

Matsumoto A, Lindsay A, Abedian B, Kaplan DL. Silk fibroin solution properties related to assembly and structure. Macromol Biosci 2008; 8: 1006–1018.10.1002/mabi.200800020Search in Google Scholar

Mayes EL, Vollrath F, Mann S. Fabrication of magnetic spider silk and other silk-fiber composites using inorganic nanoparticles. Adv Mater 1998; 10: 801–805.10.1002/(SICI)1521-4095(199807)10:10<801::AID-ADMA801>3.0.CO;2-ISearch in Google Scholar

Morgan AW, Roskov KE, Lin-Gibson S, Kaplan DL, Becker ML, Simon CG Jr. Characterization and optimization of RGD-containing silk blends to support osteoblastic differentiation. Biomaterials 2008; 29: 2556–2563.10.1016/j.biomaterials.2008.02.007Search in Google Scholar

Mukhopadhyay S, Sakthivel JC. Spider silk providing new insights in the field of high performance materials. J Ind Text 2005; 35: 91–113.10.1177/1528083705057573Search in Google Scholar

Rammensee S, Huemmerich D, Hermanson KD, Scheibel T, Bausch AR. Rheological characterization of hydrogels formed by recombinantly produced spider silk. Appl Phys A 2006; 82: 261–264.10.1007/s00339-005-3431-xSearch in Google Scholar

Rammensee S, Slotta U, Scheibel T, Bausch AR. Assembly mechanism of recombinant spider silk proteins. Proc Natl Acad Sci USA 2008; 105: 6590–6595.10.1073/pnas.0709246105Search in Google Scholar

Riekel C, Bränden C, Craig C, Ferrero C, Heidelbach F, Müller M. Aspects of x-ray diffraction on single spider fibers. Int J Biol Macromol 1999; 24: 179–186.10.1016/S0141-8130(98)00084-1Search in Google Scholar

Rising A, Hjälm G, Engström W, Johansson J. N-terminal nonrepetitive domain common to dragline, flagelliform, and cylindriform spider silk proteins. Biomacromoleclues 2006; 7: 3120–3124.10.1021/bm060693xSearch in Google Scholar

Rising A, Widhe M, Johansson J, Hedhammar M. Spider silk proteins: recent advances in recombinant production, structure- function relationships and biomedical applications. Cell Mol Life Sci 2011; 68: 169–184.10.1007/s00018-010-0462-zSearch in Google Scholar

Romer L, Scheibel T. The elaborate structure of spider silk. Prion 2008; 2: 154–161.10.4161/pri.2.4.7490Search in Google Scholar

Scheibel T. Protein fibers as performance proteins: new technologies and applications. Curr Opin Biotechnol 2005; 16: 427–433.10.1016/j.copbio.2005.05.005Search in Google Scholar PubMed

Seidel A, Liivak O, Jelinski LW. Artificial spinning of spider silk. Macromolecules 1998; 31: 6733–6736.10.1021/ma9808880Search in Google Scholar

Simmons A, Michal CA, Jelinski LW. Molecular orientation and two- component nature of the crystalline fraction of spider dragline silk. Science 1996; 271: 84–87.10.1126/science.271.5245.84Search in Google Scholar PubMed

Slotta UK, Rammensee S, Gorb S, Scheibel T. An engineered spider silk protein forms microspheres. Angew Chem Int Ed 2008; 47: 4592–4594.10.1002/anie.200800683Search in Google Scholar PubMed

Spiess K, Lammel A, Scheibel T. Recombinant spider silk proteins for applications in biomaterials. Macromol Biosci 2010; 10: 998–1007.10.1002/mabi.201000071Search in Google Scholar PubMed

Sponner A, Unger E, Grosse F, Weisshart K. Conserved C-termini of spidroins are secreted by the major ampullate glands and retained in the silk thread. Biomacromolecules 2004; 5: 840–845.10.1021/bm034378bSearch in Google Scholar PubMed

Sponner A, Vater W, Rommerskirch W, Vollrath F, Unger E, Grosse F, Weisshart K. The conserved C-termini contribute to the properties of spider silk fibroins. Biochem Biophys Res Commun 2005; 338: 897–902.10.1016/j.bbrc.2005.10.048Search in Google Scholar PubMed

Sugihara A, Sugiura K, Morita H, Ninagawa T, Tubouchi K, Tobe R, Izumiya M, Horio T, Abraham NG, Ikehara S. Promotive effects of a silk film on epidermal recovery from full-thickness skin wounds. Proc Soc Exp Biol Med 2000; 225: 58–64.10.1046/j.1525-1373.2000.22507.xSearch in Google Scholar PubMed

Sunde M, Serpell LC, Bartlam M, Fraser PE, Pepys MB, Blake CC. Common core structure of amyloid fibrils by synchrotron x-ray diffraction. J Mol Biol 1997; 273: 729–739.10.1006/jmbi.1997.1348Search in Google Scholar PubMed

Tai P-L, Hwang G-Y, Tso I-M. Inter-specific sequence conservation and intra-individual sequence variation in a spider silk gene. Int J Biol Macromol 2004; 34: 237–243.10.1016/j.ijbiomac.2004.08.002Search in Google Scholar PubMed

Takahashi Y, Gehoh M, Yuzuriha K. Structure refinement and diffuse streak scattering of silk (Bombyx mori). Int J Biol Macromol 1999; 24: 127–138.10.1016/S0141-8130(98)00080-4Search in Google Scholar

Termonia Y. Molecular modeling of stress-strain behavior of spider dragline in structural biological materials. Amsterdam, the Netherlands: Pergamon Press, 2000: 335–349.10.1016/S1470-1804(00)80015-2Search in Google Scholar

Van Beek JD, Kümmerlen J, Vollrath F, Meier BH. Supercontracted spider dragline silk: a solid state NMR study of the local structure. Int J Biol Macromol 1999; 24: 173–178.10.1016/S0141-8130(98)00083-XSearch in Google Scholar

Van Beek JD, Hess S, Vollrath F, Meier BH. The molecular structure of spider dragline silk: folding and orientation of the protein backbone. Proc Natl Acad Sci 2002; 99: 10266–10271.10.1073/pnas.152162299Search in Google Scholar

Vasir JK, Tambwekar K, Garg S. Bioadhesive microspheres as a controlled drug delivery system. Int J Pharm 2003; 255: 13–32.10.1016/S0378-5173(03)00087-5Search in Google Scholar

Vincent J. Structural biomaterials. Princeton, NJ: Princeton University Press, 1982: 204.Search in Google Scholar

Vollrath F. Biology of spider silk. Int J Biol Macromol 1999; 24: 81–88.10.1016/S0141-8130(98)00076-2Search in Google Scholar

Vollrath F, Knight DP. Liquid crystalline spinning of spider silk. Nature 2001; 410: 541–548.10.1038/35069000Search in Google Scholar PubMed

Vollrath F, Kohler T. Mechanics of silk produced by loaded spiders. Proc R Soc Biol Sci 1996; 263: 387–391.10.1098/rspb.1996.0059Search in Google Scholar

Vollrath F, Madsen B, Shao Z. The effect of spinning conditions on the mechanics of a spider’s dragline silk. Proc R Soc Biol Sci 2001; 268: 2339–2346.10.1098/rspb.2001.1590Search in Google Scholar PubMed PubMed Central

Wainwright SA. Mechanical design in organisms. Princeton, NJ: Princeton University Press, 1982: 423.10.1515/9780691218090Search in Google Scholar

Wang X, Kim HJ, Xu P, Matsumoto A, Kaplan DL. Biomaterial coatings by stepwise deposition of silk fibroin. Langmuir 2005; 21: 11335–11341.10.1021/la051862mSearch in Google Scholar PubMed

Wang X, Wenk E, Hu X, Castro GR, Meinel L, Wang X, Li C, Merkle H, Kaplan DL. Silk coatings on PLGA and alginate microspheres for protein delivery. Biomaterials 2007a; 28: 4161–4169.10.1016/j.biomaterials.2007.05.036Search in Google Scholar PubMed PubMed Central

Wang XY, Hu X, Daley A, Rabotyagova O, Cebe P, Kaplan DL. Nanolayer biomaterial coatings of silk fibroin for controlled release. J Control Release 2007b; 121: 190–199.10.1016/j.jconrel.2007.06.006Search in Google Scholar PubMed PubMed Central

Work RW. Dimensions, birefrigerences, and force-elongation behavior of major and minor ampullate silk fibers from orb-web-spinning spiders – the effect of wetting on these properties. Text Res J 1977; 47: 650–662.10.1177/004051757704701003Search in Google Scholar

Work RW, Morosoff N. A physico-chemical study of the supercontraction of spider major ampullate silk fibers. Text Res J 1982; 52: 349–356.10.1177/004051758205200508Search in Google Scholar

Xiao XX, Qian Z-G, Ki CS, Park YH, Kaplan DL, Lee SY. Native-sized recombinant spider silk protein produced in metabolically engineered Escherichia coli: results in a strong fiber. Proc Natl Acad Sci 2010; 107: 14059–14063.10.1073/pnas.1003366107Search in Google Scholar PubMed PubMed Central

Xu M, Lewis RV. Structure of protein superfiber: spider dragline silk. Proc Natl Acad Sci 1990; 87: 7120–7124.10.1073/pnas.87.18.7120Search in Google Scholar PubMed PubMed Central

Yasutomo N, Nishiyama Y, Wada M, Kuga S, Magoshi J. Mechanical properties of silk fibroin-microcrystalline cellulose composite films. J Appl Polym Sci 2002; 86: 3425–3429.10.1002/app.11370Search in Google Scholar

Received: 2014-11-15
Accepted: 2015-3-11
Published Online: 2015-5-15
Published in Print: 2015-10-1

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