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Fourier transform Raman and Fourier transform infrared spectroscopy studies of silk fibroin

Jianzhong ShaoCollege of Materials and Textiles, Zhejiang Sci-Tech University, Hangzhou, 310018, People's Republic of ChinaJinhuan ZhengCollege of Materials and Textiles, Zhejiang Sci-Tech University, Hangzhou, 310018, People's Republic of ChinaJinqiang LiuCollege of Materials and Textiles, Zhejiang Sci-Tech University, Hangzhou, 310018, People's Republic of ChinaC. M. CarrDepartment of Textiles, University of Manchester Institute of Science and Technology, P.O. Box 88, Manchester, M60 1QD, United Kingdom
2005en
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Abstract The chemical and conformational structures of Bombyx mori silk were studied with the complementary techniques of Fourier transform Raman spectroscopy and Fourier transform infrared spectroscopy. The Fourier transform Raman spectrum of silk showed strong bands for the photosensitive aromatic amino acids tyrosine, tryptophan, and phenylalanine. Intensive UV/ozone irradiation reduced the Raman intensities of the amide III band and the tyrosine signals due to peptide chain scission of the silk polymer and the photochemical changes in the tyrosine residues on the silk molecules. However, the Raman spectroscopy changes for tryptophan were less clearly defined because of peak overlapping with other amino acid signals and the low concentration of tryptophan. The Fourier transform infrared (attenuated total reflectance) technique, coupled with second‐derivative spectroscopy analysis, demonstrated a decrease in the crystallinity degree and tyrosine content of UV/ozone‐irradiated silk, as indicated by changes in the Fourier transform infrared bands of amide III doublet and tyrosine signals. © 2005 Wiley Periodicals, Inc. J Appl Polym Sci 96: 1999–2004, 2005

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