Abstract
A number of recent reviews and books on silkworm and spider silks have been published and the historical aspects of the field are reviewed therein (Livengood, 1990; Robson, 1985; Asakura and Kaplan, 1995; Kaplan et al., 1991, 1992b, 1994). Silks can be defined as externally spun fibrous protein secretions. Of the natural fibers, silks represent the only ones that are spun by the producing organism. These fibers are remarkable materials when considering their biosynthesis, processing, and functional properties. These proteins are produced within specialized glands by a variety of organisms including silkworms (and most other lepidoptera larvae), spiders, scorpions, mites, and flies. Silks differ in properties, composition, and morphology depending on the source, and in many spiders different silks are synthesized for different functions.
Access this chapter
Tax calculation will be finalised at checkout
Purchases are for personal use only
Preview
Unable to display preview. Download preview PDF.
References
Andersen SO (1970): Amino acid composition of spider silks. Comp Biochem Physiol 35:705–711
Anderson JP, Stephen-Hassard M, Martin DC (1994a): Structural evolution of genetically engineered silklike protein polymers. In: Silk Polymers: Materials Science and Biotechnology, Kaplan DL, Adams WW, Farmer B, Viney C, eds. Washington, DC: American Chemical Society Symposium Series 544
Anderson JP, Cappello J, Martin DC (1994b): Morphology and primary crystal structure of a silk-like protein polymer synthesized by genetically engineered Escherichia coli bacteria. Biopolymers 34:1049–1057
Ando Y, Okano R, Nishida K, Miyata S, Fukade E (1980): Piezoelectric and related properties of hydrated silk fibroin. Rep Prog Polymer Physics Japan 23:775–778
Asakura T, Kaplan DL (1995): ‘Silk production and processing’ In:Encyclopedia of Agricultural Science. New York: Academic Press
Asakura T, Demura M, Uyama A, Ogawa K, Komatsu K, Nicholson LK, Cross TA (1994): NMR characterization of silk proteins. In: Silk Polymers: Materials Science and Biotechology, Kaplan DL, Adams WW, Farmer B, Viney C, eds. Washington, DC: American Chemical Society Symposium Series 544
Asakura T, Watanabe Y, Uchita A, Minagawa H (1984): NMR of silk fibroin. 2. 13CNMR study of the chain dynamics and solution structure of Bombyx mori silk fibroin. Macromolecules 17:1075–1081
Asakura T, Kuzuhara A, Tabeta R, Saito H (1985): Conformation characterization of Bombyx mori silk fibroin in the solid state by high-frequency 13C cross polarization-magic angle spinning NMR, X-ray diffraction and infrared spectroscopy. Macromolecules 18:1841–1845
Asakura T, Sakaguchi R, Demura M, Manabe T, Uyama A, Ogawa K, Osanai M (1993): In vitro production of Bombyx mori silk fibroin by organ culture of the posterior silk glands; isotope labeling and fluorination of the silk fibroin. 41:245–252
Becker MA, Tuross N (1994): Initial degradation changes found in Bombyx mori silk fibroin. In: Silk Polymers: Materials Science and Biotechnology, Kaplan DL, Adams WW, Farmer B, Viney C, eds. ••: American Chemical Society Symposium Series 544
Becker MA, Mahoney DV, Lenhert PG, Eby RK, Kaplan D, Adams WW (1994): X-ray moduli of silk fibers from Nephila clavipes and Bombyx mori. In: Silk Polymers: Materials Science and Biotechnology, Kaplan DL, Adams WW, Farmer B, Viney C, eds. ••: American Chemical Society Symposium Series 544
Beckwitt R, Arcidiacono S (1994): Sequence conservation in the C-terminal region of spider silk proteins (Spidroin) from Nephila clavipes (Tetragnathidae) and Araneus bicentenarius (Araneidae). J Biol Chem 269:6661–6663
Candelas GC, Cintron JJ (1981): A spider fibroin and its synthesis. J Exp Zoology 216:1–6
Candelas GC, Lopez F (1983): Synthesis of fibroin in the cultured glands of Nephila clavipes. Comp Biochem Physiol 74:637–641
Candelas GC, Candelas T, Ortiz A, Rodriguez O (1983): Translational pauses during a spider fibroin synthesis. Biochem Biophys Res Commun 116:1033–1038
Capello J, McGrath KP (1994): Spinning of protein polymer fibers. In: Silk Polymers: Materials Science and Biotechnology, Kaplan DL, Adams WW, Farmer B, Viney C, eds. Washington, DC: American Chemical Society Symposium Series 544
Capello J, Crissman J, Dorman M, Mikolajczak M, Textor G, Marquet M, Ferrari FA (1990): Genetic engineering of structural protein polymers. Biotech Prog 6:198–202
Case ST, Smith SV (1994): Synthetic and recombinant domains from a Midge’s giant silk protein: role for disulfide bonds. In: Silk Polymers: Materials Science and Biotechnology, Kaplan DL, Adams WW, Farmer B, Viney C, eds. Washington, DC: American Chemical Society Symposium Series 544
Case ST, Powers J, Hamilton K, Burton MJ (1994): Silk and silk proteins from two aquatic insects. In: Silk Polymers: Materials Science and Biotechnology, Kaplan DL, Adams WW, Farmer B, Viney C, eds. Washington, DC: American Chemical Society Symposium Series 544
Chevallier A, Garel JP (1979): Studies on tRNA adaptation, tRNA turnover, precursor tRNA and tRNA gene distribution in Bombyx mori by using two-dimensional polyacrylamide gel electrophoresis. Biochimie 61:245–262
Colonna-Cesari F, Premilat S, Lotz B (1975): Conformational analysis of the beta sheet structure of poly-L-alanine and poly (L-alanyl-glycine). J Mol Biol 95:71–82
Couble PM, Chvillard M, Moine A, Ravel-Chapuis P, Prudhomme J-C (1985): 13:1801
Craig CL (1994): Importance of unique silk protein to the ecological and evolutionary diversity of araneid spider. In: Silk Polymers: Materials Science and Biotecnology, Kaplan DL, Adams WW, Farmer B, Viney C, eds. ••: American Chemical Society Symposium Series 544
Craig CL (1992): Trends in Ecol Evoln 7:270
Craig CL, Bernard GD (1989): Insect attraction to ultraviolet-reflecting spider webs and web decorations. Ecology 71:616–623
Cunniff PM, Fossey SA, Auerbach MA, Song JW (1994a): Mechanical properties of major ampullate gland silk fibers extracted from Nephila clavipes spiders. In: Silk Polymers: Materials Science and Biotechnology, Kaplan DL, Adams WW, Farmer B, Viney C, eds. Washington, DC: American Chemical Society Symposium Series 544
Cunniff PM, Fossey SA, Auerbach MA, Song JW, Kaplan DL, Adams WW, Eby RK, Mahoney D, Vezie DL (1994b): Mechanical and thermal properties of dragline slik from the spider Nephila clavipes. Poly Adv Technol 5:401–410
Demura M, Asakura T (1991): Porous membrane of Bombyx mori silk fibroin: structure characterization, physical properties and application to glucose oxidase immobilization. J Membrane Sci 59:39–52
Denny MW (1980): Silks—their properties and functions. In: Mechanical Properties of Biological Materials, Vincent JFV, Currey JD, eds. Washington, DC: Cambridge University Press
Denny MW, (1976): The physical properties of spider’s silk and their role in the design of orb-webs. J Exp Biol 65:483–506
Edmonds DT, Vollrath F (1992): Proc Royal Soc Lond. B248:145
Fahnestock SR (1994): Novel, recombinantly produced spider silk analogs. European Patent Filing WO 94/29450
Foelix RF (1992): Biology of Spiders. Cambridge, MA: Harvard University Press
Fossey S, Kaplan DL (1994): Molecular modeling studies on silk peptides. In: Slik Polymers: Materials Science and Biotechnology, Kaplan DL, Adams WW, Farmer B, Viney C, eds. Washington, DC: American Chemical Society Symposium Series 544
Fossey SA, Nemthy G, Gibson KD, Scheraga HA (1991): Conformational energy studies of ß-sheets of model silk fibron peptides. I. Sheets of alanine and glycine. Biopolymers 3:1529
Fossey S, Gibson KD, Nemethy G, Kaplan DL, Scheraga HA (1996): In preparation
Fraser RDB, MacRae TP (1973): Silks. In:Conformation in Fibrous Proteins. New York: Academic Press
Fraser RDB, MacRae TP, Stewart FHC, Suzuki E (1965): Poly-L-alanylglycine. J Mol Biol 11:706–712
Gage LP, Manning RF (1980a): Internal structure of the silk fibroin gene of Bombyx mori. J Biol Chem 255:9444–9450
Garel JP, Hentzen D, Schlegel M, Dirheimer G (1976): Structural studies on RNA from Bombyx mori. Biochimie 58:1089–1100
Gillespie DB, Viney C, Yager P (1994): Raman spectroscopic analysis of the secondary structure of spider silk fibers. In: Silk Polymers: Materials Science and Biotechnology, Kaplan DL, Adams WW, Farmer B, Viney C, eds. Washington, DC: American Chemical Society Symposium Series 544
Goldsmith MR, Shi J (1994): Molecular map for the silkworm: constructing new links between basic and applied research. In: Silk Polymers: Materials Science and Biotechnology, Kaplan DL, Adams WW, Farmer B, Viney C, eds. Washington, DC: American Chemical Society Symposium Series 544
Gosline JM, Denny MW, DeMont ME (1984): Spider silk as rubber. Nature 3009:551–552
Gosline JM, DeMont ME, Denny MW (1986): The structure and properties of spider silk. Endeavour 10:37–43
Hentzen D, Chevallier A, Garel JP (1981): Differential use of iso-accepting tRNASer species in silk glands of Bombyx mori. Nature 290:267–269
Hinman MB, Lewis RV (1992): Isolation of a clone encoding a second dragline silk fibroin, Nephila clavipes dragline silk is a two protein fiber. J Biol Chem 267:19320–19324
Hyde N (1984): The queen of textiles. National Georgraphic 165:3–49
Ilzuka E (1985a): Silk Thread: mechanism of spinning and its mechanical properties. J Appl Poly Sci Japan 41:173–185
Ilzuka E (1985b): Silk: an overview. J Appl Poly Sci Japan 41:163–171
Ito T (1978): Silkworm nutrition. In: The Silkworm, Tazima Y, ed. Tokyo: Kodansha
Jackson C, O’Brien JP (1995): Molecular weight distribution of Nephila clavipes dragline silk. Macromolecules 28:5975–5977
Kaplan DL, Lombardi SJ, Muller WS, Fossey SA (1991): “Silks”. In: Biomaterials: Novel Materials from Biological Sources Byrom D, ed. New York: Stockton
Kaplan DL, Fossey S, Viney C, Muller W (1992a): Self-organization (assembly) in biosynthesis of silk fibers—a hierarchical problem. In: Hierarchically Structured Materials, Aksay IA, Baer E, Sarikaya M, Tirrell DA, eds. Proc Materials Res Soc, Pittsburgh, PA
Kaplan DL, Adams WW, Viney C, Farmer B (1994): Silks: Materials Science and Biotechnology. Washington, DC: American Chemical Society Symposium Series 544
Kaplan DL, Fossey S, Mello CM, Arcidiacono S, Senecal K, Muller W, Stockwell S, Beckwitt R, Viney C, Kerkam K (1992b): Biosynthesis and processing of silk proteins. Mails Res Soc Bull 10:41–47
Kerkam K, Viney C, Kaplan DL, Lombardi SJ (1991): Liquid crystalline characteristics of natural silk secretions. Nature 349:596–598
Laible RC (1980): Fibrous armor. In: Ballistic Materials and Penetration Mechanics, Laible RC, ed. Amsterdam: Elsevier
Lewis RV, Colgin M (1995): cDNAs encoding minor ampullate spider silk proteins. European Patent Filing WO 95/25165
Lin LH, Edmonds DT, Vollrath F (1995): Structural engineering of an orb-spider’s web. Nature 273:146–148
Livengood CD (1990): Silk. In: Poymers-Fibers and Textiles: A Compendium, Kroschowitz JI, ed. New York: Wiley
Lizardi PM (1979): Discontinuous translation of silk fibroin in a reticulocyte cell-free system and in intact silk gand cells. Proc Natl Acad Sci USA 76:6211–6215
Lock R (1993): Fiber-spinnable solutions of silkworm fibroin. PCT Patent W093/15244
Lombardi SJ, Kaplan DL (1990): The amino acid composition of major ampullate gland silk (dragline) of Nephila clavipes (Araneae, Tetrgnathidae). J ArachnoI 18:297–306
Lombardi SJ, Kaplan DL (1991): The Nephila clavipes major ampullate gland silk protein, amino acid composition and detection of silk gene-related nucleic acids in the genome. Acta Zool Fennica 190:243
Lotz B, Colonna-Cesari F (1979): The chemical structure and crystalline structures of Bombyx mori silk fibroin. Biochimie 61:205–214
Lotz B, Keith HD (1971): Crystal structure of poly(L-Ala-Gly) II. J Mol Biol 61:201–215
Lucas F, Shaw JTB, Smith SG (1958): In: Advances in Protein Chemistry, Anfinsen CB, Anson ML, Bailey K, Edsall JT, eds. New York: Academic Press
Lucas F, Rudall KM (1968): In: Comprehensive Biochemistry: Extracellular and Supporting Structures, Florkin M, Stotz EH, eds. Amsterdam: Elsevier
Lucas F, Shaw JTB, Smith SG (1960): Comparative studies of fibroins I. The amino acid composition of various fibroins and its signficance in relation to their crystal structure and taxonomy. J Mol Biol 2:339–349
Lucas F, Shaw JTB, Smith SG (1962): Some amino acid sequences in the amorphous fraction of the fibroin of Bombyx mori. Biochem J 83:164–171
Mahoney DV, Vezie DL, Eby RK, Adams WW, Kaplan DL (1994): In: Silk Polymers: Materials Science and Biotechnology, Kaplan DL, Adams WW, Farmer B, Viney C, eds. Washington, DC: American Chemical Society Symposium Series 544
Magoshi J, Magoshi Y, Nakamura S (1994): Mechanism of fiber formation of silkworm. In: Silk Polymers: Materials Science and Biotechnology, Kaplan DL, Adams WW, Farmer B, Viney C, eds. Washington, DC: American Chemical Society Symposium Series 544
Magoshi J, Magoshi Y (1977): Physical properties and structure of silk. V. Thermal behavior of silk fibroin in the random-coil conformation. J Polym Sci Japan 15:1675–1683
Magoshi J, Magoshi Y, Nakamura S (1985): Crystallization, liquid crystal, and fiber formation of silk fibroin. J Appl Poly Sci 41:187–204
Manning RF, Gage LP (1978): Physical map of the Bombyx mori DNA containing the gene for silk fibroin. J Biol Chem 253:2044–2052
Manning RF, Gage LP (1980): Internal structure of the silk fibroin gene of Bombyx mori. II. Remarkable polymorphism of the organization of crystalline and amorphous coding sequences. J Biol Chem 255:9451–9457
Marsh RE, Corey RB, Paulling L (1995): An investigation of the structure of silk fibroin. Biochim Biophys Acta 16:1–34
McNamee SG, Ober CK, Jelinski LW, Ray E, Xia Y, Grubb DT (1994): Toward single-fiber diffraction of spider dragline silk from Nephila clavipes. In: Silk Polymers: Materials Science and Biotechnology, Kaplan DL, Adams WW, Farmer B, Viney C, eds. Washington, DC: American Chemical Society Symposium Series 544
Mello CM, Senecal K, Yeung B, Vouros P, Kaplan DL (1994): Initial characterization of Nephila clavipes dragline protein. In: Silk Polymers: Materials Science and Biotechnology, Kaplan DL, Adams WW, Farmer B, Viney C, eds. Washington, DC: American Chemical Society Symposium Series 544
Minoura N, Tsuada M, Nagura M (1990a): Fine structure and oxygen permeability of silk fibroin membrane treated with methanol. Polymer 31:265–269
Minoura N, Tsukada M, Nagura M (1990b): Physio-chemical properties of silk fibroin membrane as a biomaterial. Biomaterials 11:430–434
Mita K, Ichimura S, Zama M, James TC (1988): Specific codon usage pattern and its implications on the secondary structure of silk fibroin mRNA. J Mol Biol 203:917–925
Mita K, Ichimura S, James TC (1994): Highly repetitive structure and its organization of silk fibroin gene. J Mol Evol 38:583–592
Muller WS, Samuelson LA, Fossey SA, Kaplan DL (1993): Formation and characterization of Langmuir silk films. Langmuir 9:1857–1861
Nakamura S, Magoshi J, Magoshi Y (1994): Thermal properties of silk proteins in silkworms. In: Silk Polymers: Materials Science and Biotechnology, Kaplan DL, Adams WW, Farmer B, Viney C, eds. Washington, DC: American Chemical Society Symposium Series 544
Nicholson LK, Asakura T, Demura M, Cross TA (1993): A method for studying the structure of uniaxially aligned biopolymers using solid state 15N-NMR: application to Bombyx mori silk fibroin fibers. Biopolymers 33:847–861
Okamoto H, Ishikawa E, Suzuiki Y (1982): Structural analysis of sericin genes. J Biol Chem 257:15192–15199
Oshima Y, Suzuki Y (1977): Cloning of the silk fibroin genes and its flanking sequences. Proc Natl Acad Sci USA 74:5363–5367
Pachter R, Crane RL, Adams WW (1994): Approaches to modeling and property predictions of model peptides. In: Silk Polymers: Materials Science and Biotechnology, Kaplan DL, Adams WW, Farmer B, Viney C, eds. Washington, DC: American Chemical Society Symposium Series 544
Prince JT, McGrath KP, DiGirolamo CM, Kaplan DL (1995): Construction, cloning and expression of synthetic spider dragline silk DNA. Biochemistry 34:10879–10885
Robson RM (1985): Silk composition, structure and properties. In: Fiber Chemistry Handbook of Science and Technology, Vol. IV, Lewin M, Pearce E, eds. New York: Marcel Dekker
Selden PA (1989): Orb-weaving spiders in the early Cretaceous. Nature 340:711–712
Senecal K, Mello C, Kaplan DL (1996): In preparation
Shear WA, Palmer J A, Coddington J A, Bonamo PM (1989): A Devonian spinneret: early evidence of spiders and silk use. Science 246:479–481
Simmons A, Ray E, Jelinski LW (1994): Solid state 13C-NMR of Nephila clavipes dragline silk establishes structure and identity of crystalline regions. Macromolecules 27:5235–5237
Simmons AH, Michal CA, Jelinski LW (1996): Molecular orientation and two-component nature of the crystalline fraction of spider dragline silk. Science 271:84–87
Sprague KU (1975): The Bombyx mori silk proteins: characterization of large polypeptides. Biochemistry 14:925–931
Sprague KU, Roth MB, Manning RF, Gage LP (1979): Alleles of the fibroin gene coding for proteins of different lengths. Cell 17:407–413
Strydom DJ, Haylett T, Stead RH (1977): The amino-terminal sequence of silk fibroin peptide Cp—a reinvestigation. Biochem Biophys Res Commun 79:932–938
Suzuki Y, Brown DD (1972): Isolation and identification of the messenger RNA for silk fibroin from Bombyx mori. J Mol Biol 63:409–429
Suzuki Y, Oshima Y (1977): Isolation and characterization of the silk fibrion gene with its flanking sequences. Cold Spring Harbor Symp Quant Biol 42:947–957
Suzuki Y, Takiya S, Kuzuki T, Hui C-C, Matsuno K, Fukuta M, Nagata T, Ueono K (1990): Developmental regulation of silk gene expression in Bombyx mori. In: Molecular Insect Science, Gagedorn HH, ed. New York: Plenum Press
Suzuki Y, Gage LP, Brown DD (1972): The genes for silk fibroin in Bombyx mori. J Mol Biol 70:637–649
Takashasi Y (1994): Crystal structure of silk of Bombyx mori. In: Silk Polymers: Materials Science and Biotechnology, Kaplan DL, Adams WW, Farmer B, Viney C, eds. Washington, DC: American Chemical Society Symposium Series 544
Tashiro Y, Morimoto T, Matsura S, Nagata S (1968): Studies on the posterior silk gland of the silkworm, Bombyx mori. J Cell Biol 38:574–588
Termonia Y (1994): Molecular modeling of spider silk elasticity. Macromolecules 27:7378–7381
Thiel B, Kunkel D, Guess K, Viney C (1994): Composite microstructure of spider (Nephila clavipes) dragline. Mat Res Soc Symp Proc 330:21–30
Tillinghast EK, Townley MA (1994): Silk glands of Araneid spiders: selected morphological and physiological aspects. In: Silk Polymers:Materials Science and Biotechnology, Kaplan DL, Adams WW, Farmer B, Viney C, eds. Washington, DC: American Chemical Society Symposium Series 544
Tillinghast EK, Chase SF, Townley MA (1984): Water extraction by the major ampullate duct during silk formation in the spider Argiope aurantia Lucas. J Insect Physiol 30:591–596
Townley MA, Tillinghast EK (1988): Orb web recycling in Araneus cavaticus (Araneae, Araneidae) with an emphasis on the adhesive spiral component, gabamide. J Arachnol 16:303–319
Tsuijimoto Y, Suzuki Y (1979a): Structural analysis of the fibroin gene at the 5’ end and its surrounding regions. Cell 16:425–436
Tsuijimoto Y, Suzuki Y (1979b): The DNA sequence of Bombyx mori fibroin gene including the 5’ flanking, mRNA coding, entire intervening and fibroin protein coding regions. Cell 18:591–600
Valluzzi R, Gido SP, Zhang W, Muller WS, Kaplan DL (1996): A trigonal crystal structure of Bombyx mori silk incorporating a threefold helical chain conformation found at the air-water interface. Macromolecules: In press
Viney C, Huber AE, Dunaway DL, Kerkam K, Case ST (1994): Optical characterization of silk secretions and fibers. In: Silk Polymers: Materials Science and Biotechnology, Kaplan DL, Adams WW, Farmer B, Viney C, eds. Washington, DC: American Chemical Society Symposium Series 544
Vollrath F (1994): General properties of some spider silks. In: Silk Polymers: Materials Science and Biotechnology, Kaplan DL, Adams WW, Farmer B, Viney C, eds. Washington, DC: American Chemical Society Symposium Series 544
Vollrath F, Fairbrother WJ, Williams RJP, Tillinghast EK, Bernstein DT, Gallagher KS, Townley MA (1990): Compounds in the droplets of the orb spider’s viscid spiral. Nature 345:526–528
Warwicker JO (1960): Comparative studies of fibroins. II. The cystal structures of various fibroins. J Mol Biol 2:350–362
Work RW (1977): Dimension, birefringence and force-elongation behavior of major and minor ampullate silk fibers from orb-web spinning spiders—the effects of wetting on their properties. Text Res J 47:650–662
Work RW (1981): A comparative study of the supercontraction of major ampullate silk fibers of orb-web-building spiders (Araneae). J Arachnol 9:299–308
Work RW (1984): Duality in major ampullate silk and precursive material from orb-web-building spiders (Araneae). Trans American Microscopy Soc 103:113–121
Work RW, Emerson PD (1982): An apparatus and technique for the forcible silking of spiders. J Arachnol 10:1–10
Xu M, Lewis RV (1990): Structure of a protein superfiber: spider dragline silk. Proc Natl Acad Sci USA 87:7120–7124
Yamaguchi K, Kikuchi Y, Takagai T, Kikuchi A, Oyama F, Shimura K, Mizuno S (1989): Primary structure of the silk fibroin light chain determined by cDNA sequencing and peptide analysis. J Mol Biol 210:127–139
Yoshimizu H, Asakura T (1990): Preparation and characterization of silk fibroin powder and its application to enzyme immobilization. J Appl Poly Sci 40:127–134
Zemlin JC (1968): A study of the mechanical behavior of spider silks. Report 69–29-CM (AD684333) U.S. Army Natick Laboratories, Natick, MA
Editor information
Editors and Affiliations
Rights and permissions
Copyright information
© 1997 Birkhäuser boston
About this chapter
Cite this chapter
Kaplan, D.L., Mello, C.M., Arcidiacono, S., Fossey, S., Senecal, K., Muller, W. (1997). Silk. In: McGrath, K., Kaplan, D. (eds) Protein-Based Materials. Bioengineering of Materials. Birkhäuser Boston. https://doi.org/10.1007/978-1-4612-4094-5_4
Download citation
DOI: https://doi.org/10.1007/978-1-4612-4094-5_4
Publisher Name: Birkhäuser Boston
Print ISBN: 978-1-4612-8649-3
Online ISBN: 978-1-4612-4094-5
eBook Packages: Springer Book Archive