Abstract
Silk is one of the famous natural materials since ancient time due to its elegance and diverse applications. Two key proteins are hydrophilic: sericin and hydrophobic fibroin. It has unique properties like biodegradation, oxidation resistance, antibacterial and UV resistance which attract researchers. The variety of silk proteins has helped in the development of novel biomaterials and successful functioning in the treatment of various diseases. Silk proteins play an important role in the development of human tissues, skin development, regeneration of eye lenses, intervertebral disc, stem cells, nerve cells, ligament and biocompatible implants for sleep disc including anticancerous stuff. In the future, we can see more silk and its proteins based highly on advanced engineered biomaterials for the biomedical industries.
Access this chapter
Tax calculation will be finalised at checkout
Purchases are for personal use only
References
Adachi T, Tomita M, Shimizu K, Ogawa S, Yoshizato K (2006) Generation of hybrid transgenic silkworms that express Bombyx mori prolyl-hydroxylase α-subunits and human collagens in posterior silk glands: production of cocoons that contained collagens with hydroxylated proline residues. J Biotechnol 126(2):205–219
Aibibu D, Hild M, Cherif C (2016) An overview of braiding structure in medical textile: fiber-based implants and tissue engineering. In: Advances in braiding technology. Woodhead Publishing, pp 171–190
Altman GH, Diaz F, Jakuba C, Calabro T, Horan RL, Chen J, Lu H, Richmond J, Kaplan DL (2003) Silk-based biomaterials. Biomaterials 24(3):401–416
Aramwit P, Sangcakul A (2007) The effects of sericin cream on wound healing in rats. Biosci Biotechnol Biochem 71(10):2473–2477
Cassinelli C, Cascardo G, Morra M, Draghi L, Motta A, Catapano G (2006) Physical-chemical and biological characterization of silk fibroin-coated porous membranes for medical applications. Int J Artif Organs 29(9):881
Catto V, Farè S, Cattaneo I, Figliuzzi M, Alessandrino A, Freddi G, Remuzzi A, Tanzi MC (2015) Small diameter electrospun silk fibroin vascular grafts: mechanical properties, in vitro biodegradability, and in vivo biocompatibility. Mater Sci Eng C 54:101–111
Chouhan D, Chakraborty B, Nandi SK, Mandal BB (2017) Role of non-mulberry silk fibroin in deposition and regulation of extracellular matrix towards accelerated wound healing. Acta Biomater 48:157–174
De Vos WM (2015) Microbial biofilms and the human intestinal microbiome. NPJ Biofilms Microbiomes 1:15005
DeBari MK, Abbott RD (2019) Microscopic considerations for optimizing silk biomaterials. Wiley Interdiscip Rev Nanomed Nanobiotechnol 11(2):e1534
Farokhi M, Mottaghitalab F, Samani S, Shokrgozar MA, Kundu SC, Reis RL, Fatahi Y, Kaplan DL (2018) Silk fibroin/hydroxyapatite composites for bone tissue engineering. Biotechnol Adv 36(1):68–91
Freddi G, Mossotti R, Innocenti R (2003) Degumming of silk fabric with several proteases. J Biotechnol 106(1):101–112
Gauthier N, Mandon N, Renault S, Benedet F (2004) The Acrolepiopsis assectella silk cocoon: kairomonal function and chemical characterisation. J Insect Physiol 50(11):1065–1074
Gulrajani ML, Arora S, Aggarwal S (1997) Degummase treatment of spun silk fabric. Indian J Fibre Textile Res 22(2):119–123
Guziewicz NA, Massetti AJ, Perez-Ramirez BJ, Kaplan DL (2013) Mechanisms of monoclonal antibody stabilization and release from silk biomaterials. Biomaterials 34(31):7766–7775
Hardy JG, Scheibel TR (2009) Silk-inspired polymers and proteins. Biochem Soc Trans 37(4):677–681
Haupt J, GarcÃa-López JM, Chope K (2015) Use of a novel silk mesh for ventral midline hernioplasty in a mare. BMC Vet Res 11(1):58
Horan RL, Antle K, Collette AL, Wang Y, Huang J, Moreau JE, Volloch V, Kaplan DL, Altman GH (2005) In vitro degradation of silk fibroin. Biomaterials 26(17):3385–3393
Huby N, Vié V, Renault A, Beaufils S, Lefèvre T, Paquet-Mercier F, Pézolet M, Bêche B (2013) Native spider silk as a biological optical fiber. Appl Phys Lett 102(12):123702
Iizuka E, Hachimori A, Abe K, Sunohara M, Hiraide Y, Ueyama A, Kamo K, Fujiwara T, Nakamura F, Uno T (1983) Comparative study on the mechanical property of silk thread from cocoons of Bombyx mori L. Biorheology 20(5):459–470
Inoue S, Kanda T, Imamura M, Quan GX, Kojima K, Tanaka H, Tomita M, Hino R, Yoshizato K, Mizuno S, Tamura T (2005) A fibroin secretion-deficient silkworm mutant, Nd-sD, provides an efficient system for producing recombinant proteins. Insect Biochem Mol Biol 35(1):51–59
Janani G, Nandi SK, Mandal BB (2017) Functional hepatocyte clusters on bioactive blend silk matrices towards generating bioartificial liver constructs. Acta Biomater 67:167–182
Jiang J, Zhang S, Qian Z, Qin N, Song W, Sun L, Zhou Z, Shi Z, Chen L, Li X, Mao Y (2018) Protein bricks: 2D and 3D bio-nanostructures with shape and function on demand. Adv Mater 30(20):1705919
Jin HJ, Kaplan DL (2003) Mechanism of silk processing in insects and spiders. Nature 424(6952):1057
Kaplan D, Adams WW, Farmer B, Viney C (eds) (1993) Silk polymers: materials science and biotechnology. American Chemical Society
Kapoor S, Kundu SC (2016) Silk protein-based hydrogels: promising advanced materials for biomedical applications. Acta Biomater 31:17–32
Kasoju N, Bora U (2012) Silk fibroin based biomimetic artificial extracellular matrix for hepatic tissue engineering applications. Biomed Mater 7(4):045004
Kim HJ, Kim UJ, Vunjak-Novakovic G, Min BH, Kaplan DL (2005) Influence of macroporous protein scaffolds on bone tissue engineering from bone marrow stem cells. Biomaterials 26(21):4442–4452
Kludkiewicz B, KodrÃk D, Grzelak K, Nirmala X, Sehnal F (2005) Structurally unique recombinant Kazal-type proteinase inhibitor retains activity when terminally extended and glycosylated. Protein Expr Purif 43(2):94–102
Kundu B, Kurland NE, Bano S, Patra C, Engel FB, Yadavalli VK, Kundu SC (2014) Silk proteins for biomedical applications: bioengineering perspectives. Prog Polym Sci 39(2):251–267
Liu Y, Ling S, Wang S, Chen X, Shao Z (2014) Thixotropic silk nanofibril-based hydrogel with extracellular matrix-like structure. Biomater Sci 2(10):1338–1342
MacIntosh AC, Kearns VR, Crawford A, Hatton PV (2008) Skeletal tissue engineering using silk biomaterials. J Tissue Eng Regen Med 2(2–3):71–80
Marsh RE, Corey RB, Pauling L (1955) An investigation of the structure of silk fibroin. Biochim Biophys Acta 16:1–34
Meinel L, Fajardo R, Hofmann S, Langer R, Chen J, Snyder B, Vunjak-Novakovic G, Kaplan D (2005a) Silk implants for the healing of critical size bone defects. Bone 37(5):688–698
Meinel L, Hofmann S, Karageorgiou V, Kirker-Head C, McCool J, Gronowicz G, Zichner L, Langer R, Vunjak-Novakovic G, Kaplan DL (2005b) The inflammatory responses to silk films in vitro and in vivo. Biomaterials 26(2):147–155
Mita K, Ichimura S, James TC (1994) Highly repetitive structure and its organization of the silk fibroin gene. J Mol Evol 38(6):583–592
Mondal M (2007) The silk proteins, sericin and fibroin in silkworm, Bombyx mori Linn. A review. Caspian J Environ Sci 5(2):63–76
Motta A, Fambri L, Migliaresi C (2002) Regenerated silk fibroin films: thermal and dynamic mechanical analysis. Macromol Chem Phys 203(10–11):1658–1665
Murphy AR, John PS, Kaplan DL (2008) Modification of silk fibroin using diazonium coupling chemistry and the effects on hMSC proliferation and differentiation. Biomaterials 29(19):2829–2838
Okazaki Y, Kakehi S, Xu Y, Tsujimoto K, Sasaki M, Ogawa H, Kato N (2010) Consumption of sericin reduces serum lipids, ameliorates glucose tolerance and elevates serum adiponectin in rats fed a high-fat diet. Biosci Biotechnol Biochem 74(8):1534–1538
Omenetto FG, Kaplan DL (2008) A new route for silk. Nat Photonics 2:641–643
Omenetto FG, Kaplan DL (2010) New opportunities for an ancient material. Science 329(5991):528–531
Panda N, Bissoyi A, Pramanik K, Biswas A (2015) Development of novel electrospun nanofibrous scaffold from P. ricini and A. mylitta silk fibroin blend with improved surface and biological properties. Mater Sci Eng C 48:521–532
Ratner BD, Hoffman AS, Schoen FJ, Lemons JE (2004) Biomaterials science: an introduction to materials in medicine. Elsevier
Rockwood DN, Preda RC, Yücel T, Wang X, Lovett ML, Kaplan DL (2011) Materials fabrication from Bombyx mori silk fibroin. Nat Protoc 6(10):1612
RodrÃguez-Lozano FJ, GarcÃa-Bernal D, Aznar-Cervantes S, Ros-Roca MA, Algueró MC, Atucha NM, Lozano-GarcÃa AA, Moraleda JM, Cenis JL (2014) Effects of composite films of silk fibroin and graphene oxide on the proliferation, cell viability and mesenchymal phenotype of periodontal ligament stem cells. J Mater Sci Mater Med 25(12):2731–2741
Saric M, Scheibel T (2019) Engineering of silk proteins for materials applications. Curr Opin Biotechnol 60:213–220
Seo CW, Um IC, Rico CW, Kang MY (2011) Antihyperlipidemic and body fat-lowering effects of silk proteins with different fibroin/sericin compositions in mice fed with high fat diet. J Agric Food Chem 59(8):4192–4197
Shao Z, Vollrath F (2002) Materials: surprising strength of silkworm silk. Nature 418(6899):741
Singh MK, Varun VK, Behera BK (2011) Cosmetotextiles: state of art. Fibers Text East Eur 19(4):27–33
Sinohara H (1979) Glycopeptides isolated from sericin of the silkworm, Bombyx mori. Comp Biochem Physiol Part B Comp Biochem 63(1):87–91
Song C, Yang Z, Zhong M, Chen Z (2013) Sericin protects against diabetes-induced injuries in sciatic nerve and related nerve cells. Neural Regen Res 8(6):506
Tanaka K, Inoue S, Mizuno S (1999) Hydrophobic interaction of P25, containing Asn-linked oligosaccharide chains, with the HL complex of silk fibroin produced by Bombyx mori. Insect Biochem Mol Biol 29(3):269–276
Tokutake S (1980) Isolation of the smallest component of silk protein. Biochem J 187(2):413–417
Totten JD, Wongpinyochit T, Carrola J, Duarte IF, Seib FP (2019) PEGylation-dependent metabolic rewiring of macrophages with silk fibroin nanoparticles. ACS Appl Mater Interfaces 11(16):14515–14525
Tsukada M, Komoto T, Kawai T (1979) Confirmation of liquid silk sericin. Polym J 11(6):503
Vollrath F, Knight DP (2001) The liquid crystalline spinning of spider silk. Nature 410(6828):541
Vollrath F, Porter D (2006) Spider silk as a model biomaterial. Appl Phys A 82(2):205–212
Vootla SK, Su CC, Masanakatti SI (2015) Self-assembled nanoparticles prepared from Tasar Antherea mylitta silk sericin. In: Biomedical applications of natural proteins. Springer, New Delhi, pp 65–77
Wang X, Zhang X, Castellot J, Herman I, Iafrati M, Kaplan DL (2008) Controlled release from multilayer silk biomaterial coatings to modulate vascular cell responses. Biomaterials 29(7):894–903
Wongpanit P, Pornsunthorntawee O, Rujiravanit R (2012) Silk fiber composites. Natural polymers: composites. R Soc Chem, Cambridge, pp 219–222
Wongpinyochit T, Uhlmann P, Urquhart AJ, Seib FP (2015) PEGylated silk nanoparticles for anticancer drug delivery. Biomacromolecules 16(11):3712–3722
Wu X, Hou J, Li M, Wang J, Kaplan DL, Lu S (2012) Sodium dodecyl sulfate-induced rapid gelation of silk fibroin. Acta Biomater 8(6):2185–2192
Yin Z, Wu F, Xing T, Yadavalli VK, Kundu SC, Lu S (2017) A silk fibroin hydrogel with reversible sol-gel transition. RSC Adv 7(39):24085–24096
Yukuhiro K, Kanda T, Tamura T (1997) Preferential codon usage and two types of repetitive motifs in the fibroin gene of the Chinese oak silkworm, Antheraea pernyi. Insect Mol Biol 6(1):89–95
Zhang YQ (2002) Applications of natural silk protein sericin in biomaterials. Biotechnol Adv 20(2):91–100
Zhao JG, Zhang YQ (2015) Inhibition of the flavonoid extract from silkworm cocoons on DMBA/UVB-induced skin damage and tumor promotion in BALB/c mice. Toxicol Res 4(4):1016–1024
Zhao HP, Feng XQ, Yu SW, Cui WZ, Zou FZ (2005) Mechanical properties of silkworm cocoons. Polymer 46(21):9192–9201
Zhao HP, Feng XQ, Cui WZ, Zou FZ (2007) Mechanical properties of silkworm cocoon pelades. Eng Fract Mech 74(12):1953–1962
Zhou CZ, Confalonieri F, Esnault C, Zivanovic Y, Jacquet M, Janin J, Perasso R, Li ZG, Duguet M (2003) The 62-kb upstream region of Bombyx mori fibroin heavy chain gene is clustered of repetitive elements and candidate matrix association regions. Gene 312:189–195
Acknowledgements
Authors are indebted to Dr. D.S. Kothari Fellowship, BSR, UGC, New Delhi, India (grant No.F.4-2/2006 (BSR)/BL/17-18/0549), for the financial support.
Author information
Authors and Affiliations
Editor information
Editors and Affiliations
Rights and permissions
Copyright information
© 2020 Springer Nature Switzerland AG
About this chapter
Cite this chapter
Kumar, D., Shrivastava, S., Gong, C., Shukla, S. (2020). Silk: An Amazing Biomaterial for Future Medication. In: Kumar, D., Shahid, M. (eds) Natural Materials and Products from Insects: Chemistry and Applications. Springer, Cham. https://doi.org/10.1007/978-3-030-36610-0_3
Download citation
DOI: https://doi.org/10.1007/978-3-030-36610-0_3
Published:
Publisher Name: Springer, Cham
Print ISBN: 978-3-030-36609-4
Online ISBN: 978-3-030-36610-0
eBook Packages: Biomedical and Life SciencesBiomedical and Life Sciences (R0)