Analysis of structural properties and formation of Sericin fiber by infrared spectroscopy

Journal of Insect Biotechnology and Sericology

Volumn 72, Issue 3, 2003, Pages 157-162

  Teramoto, Hidetoshi ^a   Miyazawa, Mitsuhiro ^a  

^a NATIONAL INSTITUTE OF AGROBIOLOGICAL SCIENCES   (Japan)

Author keywords

ATR FTIR; Fiber formation; Orientation; Secondary structure; Sericin

Indexed keywords

ATR FTIR; DRYING PROCESS; FIBER FORMATION; FOURIER SELF-DECONVOLUTION; SECONDARY STRUCTURES; SERICIN; SILK PROTEINS; STRUCTURAL TRANSITIONS;

CRYSTAL ORIENTATION; DRYING; FIBERS; FOURIER TRANSFORM INFRARED SPECTROSCOPY;

SPINNING (FIBERS);

ANIMALIA; BOMBYX MORI;

FIBER ORIENTATION; FIBER PROPERTY; SILK FIBER; SPECTROSCOPY; STRUCTURAL PROPERTY;

EID: 0346334779     PISSN: 13468073     EISSN: None     Source Type: Journal    
DOI: None     Document Type: Article

References (23)

1. 13C CP/MAS NMR study on structural heterogeneity in Bombyx mori silk fiber and their generation by stretching. Protein Sci. 11, 2706-2713.
2. Byler, D.M., and Susi, H. (1986) Examination of the secondary structure of proteins by deconvolved FTIR spectra. Biopolymers 25, 469-487.
3. Dong, A., Huang, P., and Caughey, W.S. (1990) Protein secondary structures in water from second-derivative amide I infrared spectra. Biochemistry 29, 3303-3308.
4. Fedič, R., Žurovec, M., and Sehnal, F. (2002) The silk of Lepidoptera. J. Insect Biotechnol. Sericol. 71, 1-15.
5. Gamo, T., Inokuchi, T., and Laufer, H. (1977) Polypeptides of fibroin and sericin secreted from the different sections of the silk gland in Bombyx mori. Insect Biochem. 7, 285-295.
6. Gamo, T. (1982) Genetic variants of the Bombyx mori silkworm encoding sericin proteins of different lengths. Biochem. Genet. 20, 165-177.
7. Garel, A., Deleage, G., and Prudhomme, J.C. (1997) Structure and organization of the Bombyx mori sericin 1 gene and of the sericins 1 deduced from the sequence of the Ser 1B cDNA. Insect Biochem. Molec. Biol. 27, 469-477.
8. Jackson, M., and Mantsch, H.H. (1991) Protein secondary structure from FT-IR spectroscopy: correlation with dihedral angles from three-dimensional Ramachandran plots. Can. J. Chem. 69, 1639-1642.
9. Jackson, M., and Mantsch, H.H. (1995) The use and misuse of FTIR spectroscopy in the determination of protein structure. Crit. Rev. Biochem. Mol. Biol. 30, 95-120.
10. Komatsu, K. (1975) Studies on dissolution behaviors and structural characteristics of silk sericin. Bull. Seric. Exp. Stn. 26, 135-256 (in Japanese).
11. Michaille, J.J., Garel, A., and Prudhomme, J.C. (1990) Cloning and characterization of the highly polymorphic Ser2 gene of Bombyx mori. Gene 86, 177-184.
12. Miyazawa, M., Sonoyama, M., and Saito, H. (2000) FT-IR studies on secondary structures of wild silkworm fibroin films. Int. J. Wild Silkmoth Silk 5, 47-50.
13. Miyazawa, T., and Blout, E.R. (1961) The infrared spectra of polypeptides in various conformations: amide I and II bands. J. Am. Chem. Soc. 83, 712-719.
14. Okamoto, H., Ishikawa, E., and Suzuki, Y. (1982) Structural analysis of sericin genes. Homologies with fibroin gene in the 5' flanking nucleotide sequences. J. Biol. Chem. 257, 15192-15199.
15. Sinohara, H. (1979) Glycopeptides isolated from sericin of the silkworm, Bombyx mori. Comp. Biochem. Physiol. 63B, 87-91.
16. Sonoyama, M., Miyazawa, M., Katagiri, G., and Ishida, H. (1997) Dynamic FT-IR spectroscopic studies of silk fibroin films. Appl. Spectrosc. 51, 545-547.
17. Surewicz, W.K., and Mantsch, H.H. (1988) New insight into protein secondary structure from resolution-enhanced infrared spectra. Biochim. Biophys. Acta 952, 115-130.
18. Surewicz, W.K., Mantsch, H.H., and Chapman, D. (1993) Determination of protein secondary structure by Fourier transform infrared spectroscopy: a critical assessment. Biochemistry 32, 389-394.
19. Suzuki, E. (1967) A quantitative study of the amide vibrations in the infra-red spectrum of silk fibroin. Spectrochim. Acta 23A, 2303-2308.
20. Tretinnikov, O.N., and Tamada, Y. (2001) Influence of casting temperature on the near-surface structure and wettability of cast silk fibroin films. Langmuir 17, 7406-7413.
21. Yamamoto, T., Mase, K., Miyajima, T., and Hara, K. (2001) Breed of silkworm capable of producing sericin in large amount. Japanese Patent 2001-245550.
22. Yamamoto, T., Miyajima, T., Mase, K., and Iizuka, T. (2002) Breeding of the silkworm race "Sericin-hope" secreting silk protein in which sericin is contained in high concentration. In Annual Report 2002, pp. 24-25, National Institute of Agrobiological Sciences, Tsukuba.
23. Zhang, Y-Q. (2002) Applications of natural silk protein sericin in biomaterials. Biotech. Adv. 20, 91-100.