Silk Fibroin Bombyx Mori

Asakura, T., Sakaguchi, R., Demura, M., Manabe, T., Uyama, A., Ogawa, K., and 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. Biotech-nol. Bioeng. 41, 245-252. 

Ha, S. W., Gracz, H. S., Tonelli, A. E., and Hudson, S. M. (2005). Structural study of irregular amino acid sequences in the heavy chain of Bombyx mori silk fibroin. Biomacromolecules 6, 2563-2569. 

Inoue, S. I., Magoshi, J., Tanaka, T., Magoshi, Y., and Becker, M. (2000b). Atomic force microscopy Bombyx mori silk fibroin molecules and their higher order structure. /. Polym. Sci. BPolym. Phys. 38, 1436-1439. 

Lazo, N. D., and Downing, D. T. (1999). Crystalline regions of Bombyx mori silk fibroin may exhibit beta-turn and beta-helix conformations. Macromolecules 32, 4700-4705. Lee, K. H. (2004). Silk sericin retards the crystallization of silk fibroin. Macromol. Rapid Commun. 25, 1792-1796. 

Monti, P., Taddei, P., Freddi, G., Asakura, T., and Tsukada, M. (2001). Raman spectroscopic characterization of Bombyx mori silk fibroin Raman spectrum of silk I. J. Raman Spectrosc. 32, 103—107. 

Yang, Y. H., Shao, Z. Z., Chen, X., and Zhou, P. (2004). Optical spectroscopy to investigate the structure of regenerated Bombyx mori silk fibroin in solution. Biomacromolecules 5, 773-779. 

Demura M, Asakura T, Kuroo T. Immobilization of biocatalysts with bombyx mori silk fibroin by several kinds of physical treatment and its application to glucose sensors. Biosensors 1989, 4, 361-372. 

Asakura, T., Sugino, R., Okumura, T., and Nakazawa, Y. "The role of irregular unit, GAAS, on the secondary structure of Bombyx mori silk fibroin studied with C-13 CP/MAS NMR and wide-angle X-ray scattering". Protein Sci. 11(8), 1873-1877 (2002). 

Asakura, T., Suita, K., Kameda, T., Afonin, S., and Ulrich, A.S. "Structural role of tyrosine in Bombyx mori silk fibroin, studied by solid-state NMR and molecular mechanics on a model peptide prepared as silk I and II". Magn. Reson. Chem. 42(2), 258-266 (2004). 

Gotoh, Y., Tsukada, M., and Minoura, N. "Effect of the chemical modification of the arginyl residue in Bombyx mori silk fibroin on the attachment and growth of fibroblast cells".. Biomed. Mater. Res. 39(3), 351-357 (1998). 

Ha, S.W., Park, Y.H., and Hudson, S.M. "Dissolution of Bombyx mori silk fibroin in the calcium nitrate tetrahydrate-methanol system and aspects of wet spinning of fibroin solution". 

Jin, H.J., Park, J., Valluzzi, R., Cebe, P., and Kaplan, D.L. "Biomaterial films of Bombyx mori silk fibroin with polyethylene oxide)". Biomacromolecules 5(3), 711-717 (2004). 

Marsano, E., Corsini, P., Arosio, C., Boschi, A., Mormino, M., and Freddi, G. "Wet spinning of Bombyx mori silk fibroin dissolved in N-methyl morpholine N-oxide and properties of regenerated fibres". Int. J. Biol. Macromol. 37(4), 179-188 (2005). 

Yao, J.M., Masuda, H., Zhao, C.H., and Asakura, T. "Artificial spinning and characterization of silk fiber from Bombyx mori silk fibroin in hexafluoroacetone hydrate". Macromolecules 35(1), 6-9 (2002). 

Xie F et al (2006) Effect of shearing on formation of silk fibers from regenerated Bombyx mori silk fibroin aqueous solution. Int J Biol Macromol 38(3-5) 284-288 Li C et al (2006) Electrospun silk-BMP-2 scaffolds for bone tissue engineering. Biomaterials 27(16) 3115-3124... 

Some natural fibrous proteins and sequential model polypeptides have been used as follows (1) Tussah Antheraea perni silk fibroin [a-helix form], (2) Bombyx mori silk fibroin [silk I and II forms], (3) poly(L-alanyL-glycine) [Ala-Gly]i2 [silk I and II], (4) collagen fibril [triple-strand helix], and (5) poly(L-prolyl-L-alanyL-glycine) [Pro-Ala-Gly [triple-strand helix]. 

Now it is clear that the H chemical shift reflects the conformation of model polypeptide [Ala-Gly] 12 and natural silk fibroins such as Tussah Antheraea pernyi and Bombyx mori silk fibroins. It is confirmed that the well-defined [Ala-Gly] 12 is a suitable model for the structural study of natural silk fibroins (silk I and silk II forms) using high-resolution solid-state NMR. As a result, the H peak assignment of the silk fibroins on the basis of the conformation-dependent H chemical shifts of model polypeptides can be determined utilizing H CRAMPS NMR and H- C 2D HETCOR NMR, as described in this section. The chemical shift results of model polypeptides [Ala-Gly] 12 synthesized by Shoji et al. play an important role in determining new structures for silk I and silk II forms, as very recently proposed by Lazo and Downing. ... 

H.J. Jin, J. Park, R. Valluzzi, P. Cebe, D.L. Kaplan, Biomaterial films of Bombyx mori silk fibroin with poly(ethylene oxide). Biomacromolecules 5(2004)711-717. 

Asakura, T. Demura, M. Date, T. Miyashita, N. Ogawa, K. Williamson, M.P. NMR study of silk I structure of Bombyx mori silk fibroin with N-15- and C-13-NMR chemical shift contour plots. Biopolymers. 41 193-203 (1997). 

Becker, M.A. Tuross, N. Initial degradation changes found in Bombyx mori silk fibroins. In Silk Polymers Materials Science and Biotechnology. Kaplan, D.L. Adams, W.W. Farmer, B. Viney, C. Eds., American Chem. Soc. Symposium Series, 544 (1994). 

Demura, M. Asakura, T. Porous membrane of Bombyx mori silk fibroins Structure characterization, physical properties and application to glucose oxidase immobilization. J. Membr. Sci. 59 39-52 (1991). 

Structure of Bombyx mori Silk Fibroin before Spinning in Silkworm... 

Zhou, G., Shao, Z., Knight, D.P., Yan, J., and Chen, X. Silk (2009) Fibers extraded artificially from aqueous solutions of regenerated Bombyx Mori silk fibroin are tougher than their natural counterparts. Advanced Materials, 21, 366-370. 

Rockwood DN, Preda RC, Yticel T, Wang X, Lovett ML, Kaplan DL. Materials fabrication from Bombyx mori silk fibroin. Nat Protoc 2011 6 1612-31. 

A detailed structure for commercial silk fibroin (Bombyx mori) has recently been formulated in these Laboratories (Marsh, Corey Pauling, 1955). A prominent feature of the structure of Bombyx mori silk fibroin is the occurrence of glycine as alternate residues along the polypeptide chains. 

Mathur, A.B., ToneUi, A.E., Rathke, T., Hudson, S., 1997. The dissolution and characterization of Bombyx mori silk fibroin in calcium nitrate-methanol solution and the regeneration of films. Biopolymers 42 (1), 61—74. 

Rockwood, D.N., Preda, R.C., Yiicel, T., Wang, X., Lovett, M.L., Kaplan, D.L., 2011. Materials fabrication from Bombyx mori silk fibroin. Nature Protocols 6 (10), 1612-1631. 

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