期刊论文详细信息
Journal of Translational Medicine
Preparation and characterization of silk fibroin as a biomaterial with potential for drug delivery
Yu-zhang Wu1  Xia Yang1  Wei Zhou1  Bing Ni1  Hao-hao Zhang1  Fang-yin Dai3  Ling-ling Li2  Hao Zhang1 
[1]Institute of Immunology Third Military Medical University, Chongqing, 400038, Peoples Republic of China
[2]Biochemistry engineering department, Chongqing Industry & Trade Polytechnic, Chongqing, 408000, Peoples Republic of China
[3]State Key Laboratory of Silkworm Genome Biology, Southwest University, Chongqing, 400715, Peoples Republic of China
关键词: Biomaterial;    Drug delivery;    Crystalline structure;    Calcium-alcohol solutions;    Silk fibroin;   
Others  :  1205964
DOI  :  10.1186/1479-5876-10-117
 received in 2012-01-29, accepted in 2012-05-21,  发布年份 2012
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【 摘 要 】

Background

Degummed silk fibroin from Bombyx mori (silkworm) has potential carrier capabilities for drug delivery in humans; however, the processing methods have yet to be comparatively analyzed to determine the differential effects on the silk protein properties, including crystalline structure and activity.

Methods

In this study, we treated degummed silk with four kinds of calcium-alcohol solutions, and performed secondary structure measurements and enzyme activity test to distinguish the differences between the regenerated fibroins and degummed silk fibroin.

Results

Gel electrophoresis analysis revealed that Ca(NO3)2-methanol, Ca(NO3)2-ethanol, or CaCl2-methanol treatments produced more lower molecular weights of silk fibroin than CaCl2-ethanol. X-ray diffraction and Fourier-transform infrared spectroscopy showed that CaCl2-ethanol produced a crystalline structure with more silk I (α-form, type II β-turn), while the other treatments produced more silk II (β-form, anti-parallel β-pleated sheet). Solid-State 13C cross polarization and magic angle spinning-nuclear magnetic resonance measurements suggested that regenerated fibroins from CaCl2-ethanol were nearly identical to degummed silk fibroin, while the other treatments produced fibroins with significantly different chemical shifts. Finally, enzyme activity test indicated that silk fibroins from CaCl2-ethanol had higher activity when linked to a known chemotherapeutic drug, L-asparaginase, than the fibroins from other treatments.

Conclusions

Collectively, these results suggest that the CaCl2-ethanol processing method produces silk fibroin with biomaterial properties that are appropriate for drug delivery.

【 授权许可】

   
2012 Zhang et al.; licensee BioMed Central Ltd.

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【 参考文献 】
  • [1]Omenetto FG, Kaplan DL: New opportunities for an ancient material. Science 2010, 329:528-531.
  • [2]Lovett M, Eng G, Kluge JA, Cannizzaro C, Vunjak-Novakovic G, Kaplan DL: Tubular silk scaffolds for small diameter vascular grafts. Organogenesis 2010, 6:217-224.
  • [3]Altman GH, Diaz F, Jakuba C, Calabro T, Horan RL, Chen J, Lu H, Richmond J, Kaplan DL: Silk-based biomaterials. Biomaterials 2003, 24:401-416.
  • [4]Leal-Egana A, Scheibel T: Silk-based materials for biomedical applications. Biotechnol Appl Biochem 2010, 55:155-167.
  • [5]Mauney JR, Cannon GM, Lovett ML, Gong EM, Di Vizio D, Gomez P 3rd, Kaplan DL, Adam RM, Estrada CR Jr: Evaluation of gel spun silk-based biomaterials in a murine model of bladder augmentation. Biomaterials 2011, 32:808-818.
  • [6]Ali MM, Arumugam SB: Effect of crude extract of Bombyx mori coccoons in hyperlipidemia and atherosclerosis. J Ayurveda Integr Med 2011, 2:72-78.
  • [7]Zhang YQ, Ma Y, Xia YY, Shen WD, Mao JP, Zha XM, Shirai K, Kiguchi K: Synthesis of silk fibroin-insulin bioconjugates and their characterization and activities in vivo. J Biomed Mater Res B Appl Biomater 2006, 79:275-283.
  • [8]Lu S, Wang X, Lu Q, Hu X, Uppal N, Omenetto FG, Kaplan DL: Stabilization of enzymes in silk films. Biomacromolecules 2009, 10:1032-1042.
  • [9]Zhang YQ, Zhou WL, Shen WD, Chen YH, Zha XM, Shirai K, Kiguchi K: Synthesis, characterization and immunogenicity of silk fibroin-L-asparaginase bioconjugates. J Biotechnol 2005, 120:315-326.
  • [10]Chatterjee S, Barbora L, Cameotra SS, Mahanta P, Goswami P: Silk-fiber immobilized lipase-catalyzed hydrolysis of emulsified sunflower oil. Appl Biochem Biotechnol 2009, 157:593-600.
  • [11]Inoue S, Matsunaga Y, Iwane H, Sotomura M, Nose T: Entrapment of phenylalanine ammonia-lyase in silk fibroin for protection from proteolytic attack. Biochem Biophys Res Commun 1986, 141:165-170.
  • [12]Greish K, Frandsen J, Scharff S, Gustafson J, Cappello J, Li D, O'Malley BW Jr, Ghandehari H: Silk-elastinlike protein polymers improve the efficacy of adenovirus thymidine kinase enzyme prodrug therapy of head and neck tumors. J Gene Med 2010, 12:572-579.
  • [13]Zhu ZH, Ohgo K, Asakura T: Preparation and characterization of regenerated Bombyx mori silk fibroin fiber with high strength. Express Polymer Letters 2008, 2:885-889.
  • [14]Ha SW, Park YH, Hudson SM: Dissolution of Bombyx mori silk fibroin in the calcium nitrate tetrahydrate-methanol system and aspects of wet spinning of fibroin solution. Biomacromolecules 2003, 4:488-496.
  • [15]Ha SW, Tonelli AE, Hudson SM: Structural studies of Bombyx mori silk fibroin during regeneration from solutions and wet fiber spinning. Biomacromolecules 2005, 6:1722-1731.
  • [16]Zhang YQ, Tao ML, Shen WD, Zhou YZ, Ding Y, Ma Y, Zhou WL: Immobilization of L-asparaginase on the microparticles of the natural silk sericin protein and its characters. Biomaterials 2004, 25:3751-3759.
  • [17]Lotz B, Colonna Cesari F: The chemical structure and the crystalline structures of Bombyx mori silk fibroin. Biochimie 1979, 61:205-214.
  • [18]Tanaka K, Inoue S, Mizuno S: Hydrophobic interaction of P25, containing Asn-linked oligosaccharide chains, with the H-L complex of silk fibroin produced by Bombyx mori. Insect Biochem Mol Biol 1999, 29:269-276.
  • [19]Chuan Xin Liang KH: Improvements of the physical properties of fibroin membranes with sodium alginate. J Appl Polym Sci 1992, 45:1937-1943.
  • [20]Anshu Bagga Mathur AT, Thomas Rathke, Sam Hudson: The dissolution and characterization of Bombyx mori silk fibroin in calcium nitrate-methanol solution and the regeneration of films. Biopolymers 1997, 42:61-74.
  • [21]Freddi G, Pessina G, Tsukada M: Swelling and dissolution of silk fibroin (Bombyx mori) in N-methyl morpholine N-oxide. Int J Biol Macromol 1999, 24:251-263.
  • [22]Meinel L, Hofmann S, Karageorgiou V, Kirker-Head C, McCool J, Gronowicz G, Zichner L, Langer R, Vunjak-Novakovic G, Kaplan DL: The inflammatory responses to silk films in vitro and in vivo. Biomaterials 2005, 26:147-155.
  • [23]Tang Y, Cao C, Ma X, Chen C, Zhu H: Study on the preparation of collagen-modified silk fibroin films and their properties. Biomed Mater 2006, 1:242-246.
  • [24]Lu Q, Hu X, Wang X, Kluge JA, Lu S, Cebe P, Kaplan DL: Water-insoluble silk films with silk I structure. Acta Biomater 2010, 6:1380-1387.
  • [25]He SJ, Valluzzi R, Gido SP: Silk I structure in Bombyx mori silk foams. Int J Biol Macromol 1999, 24:187-195.
  • [26]Zhu Z, Kikuchi Y, Kojima K, Tamura T, Kuwabara N, Nakamura T, Asakura T: Mechanical properties of regenerated Bombyx mori silk fibers and recombinant silk fibers produced by transgenic silkworms. J Biomater Sci Polym Ed 2010, 21:395-411.
  • [27]Yao J, Asakura T: Synthesis and structural characterization of silk-like materials incorporated with an elastic motif. J Biochem 2003, 133:147-154.
  • [28]Zhao C, Yao J, Masuda H, Kishore R, Asakura T: Structural characterization and artificial fiber formation of Bombyx mori silk fibroin in hexafluoro-iso-propanol solvent system. Biopolymers 2003, 69:253-259.
  • [29]Fraser RD, MacRae TP, Stewart FH: Poly-l-alanylglycyl-l-alanylglycyl-l-serylglycine: a model for the crystalline regions of silk fibroin. J Mol Biol 1966, 19:580-582.
  • [30]Laemmli UK: Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 1970, 227:680-685.
  • [31]Killander D, Dohlwitz A, Engstedt L, Franzen S, Gahrton G, Gullbring B, Holm G, Holmgren A, Hoglund S, Killander A, et al.: Hypersensitive reactions and antibody formation during L-asparaginase treatment of children and adults with acute leukemia. Cancer 1976, 37:220-228.
  • [32]Wilson D, Valluzzi R, Kaplan D: Conformational transitions in model silk peptides. Biophys J 2000, 78:2690-2701.
  • [33]Zhang K, Fan L, Yan Z, Yu Q, Mo X: Electrospun Biomimic Nanofibrous Scaffolds of Silk Fibroin/Hyaluronic Acid for Tissue Engineering. J Biomater Sci Polym Ed 2011, 22:1069-1082.
  • [34]Teramoto H, Miyazawa M: Molecular orientation behavior of silk sericin film as revealed by ATR infrared spectroscopy. Biomacromolecules 2005, 6:2049-2057.
  • [35]Huang J, Wong C, George A, Kaplan DL: The effect of genetically engineered spider silk-dentin matrix protein 1 chimeric protein on hydroxyapatite nucleation. Biomaterials 2007, 28:2358-2367.
  • [36]Mandal BB, Kundu SC: Biospinning by silkworms: silk fiber matrices for tissue engineering applications. Acta Biomater 2010, 6:360-371.
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