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Diffuse reflectance spectroscopy of fibrous proteins

journal contribution
posted on 2012-09-01, 00:00 authored by K R Millington
UV–visible diffuse reflectance (DR) spectra of the fibrous proteins wool and feather keratin, silk fibroin and bovine skin collagen are presented. Natural wool contains much higher levels of visible chromophores across the whole visible range (700–400 nm) than the other proteins and only those above 450 nm are effectively removed by bleaching. Both oxidative and reductive bleaching are inefficient for removing yellow chromophores (450–400 nm absorbers) from wool. The DR spectra of the four UV-absorbing amino acids tryptophan, tyrosine, cystine and phenylalanine were recorded as finely ground powders. In contrast to their UV–visible spectra in aqueous solution where tryptophan and tyrosine are the major UV absorbing species, surprisingly the disulphide chromophore of solid cystine has the strongest UV absorbance measured using the DR remission function F(R)∞. The DR spectra of unpigmented feather and wool keratin appear to be dominated by cystine absorption near 290 nm, whereas silk fibroin appears similar to tyrosine. Because cystine has a flat reflectance spectrum in the visible region from 700 to 400 nm and the powder therefore appears white, cystine absorption does not contribute to the cream colour of wool despite the high concentration of cystine residues near the cuticle surface. The disulphide absorption of solid l-cystine in the DR spectrum at 290 nm is significantly red shifted by ~40 nm relative to its wavelength in solution, whereas homocystine and lipoic acid showed smaller red shifts of 20 nm. The large red shift observed for cystine and the large difference in intensity of absorption in its UV–visible and DR spectra may be due to differences in the dihedral angle between the crystalline solid and the solvated molecules in solution.

History

Journal

Amino Acids

Volume

43

Issue

3

Pagination

1277 - 1285

Publisher

Springer Wien

Location

Wien, Austria

ISSN

0939-4451

eISSN

1438-2199

Language

eng

Publication classification

C1.1 Refereed article in a scholarly journal

Copyright notice

2012, Springer-Verlag