ATR-FTIR spectroscopy as a way to identify natural protein-based materials, tortoiseshell and horn, from their protein-based imitation, galalith.

This paper presents a new totally non-destructive methodology, for the identification of protein-based materials, tortoiseshell, horn and galalith, on heritage objects. Attenuated total reflexion (ATR) infrared spectroscopy combined to a deconvolution procedure of amide I band was performed to characterize the secondary structure of these materials and allows us to identify each material. The component at 1639 cm(-1), attributed to the amide group involved in hydrated random-coil domains, allows us to distinguish horn from galalith and tortoiseshell. A second component, at 1614 cm(-1), assigned to amide group involved in protein self-association, allows us to differentiate galalith and tortoiseshell. This differentiation is applicable to both raw and manufactured materials. Then, we applied our models to identify what unknown object was made of.

[1]  D. Horne Casein structure, self-assembly and gelation , 2002 .

[2]  D. Marsh,et al.  Investigation of secondary and tertiary structural changes of cytochrome c in complexes with anionic lipids using amide hydrogen exchange measurements: an FTIR study. , 1993, Biophysical journal.

[3]  H. Susi,et al.  Raman Spectroscopic Study of Casein Structure , 1988 .

[4]  D A Parry,et al.  The molecular structure of reptilian keratin. , 1996, International journal of biological macromolecules.

[5]  Abadie,et al.  Chymotrypsin Adsorption on Montmorillonite: Enzymatic Activity and Kinetic FTIR Structural Analysis. , 1999, Journal of colloid and interface science.

[6]  H. Edwards,et al.  FT-Raman spectroscopic study of keratotic materials: horn, hoof and tortoiseshell. , 1998, Spectrochimica acta. Part A, Molecular and biomolecular spectroscopy.

[7]  H. M. Farrell,et al.  Secondary structure of bovine alphaS2-casein: theoretical and experimental approaches. , 2001, Journal of dairy science.

[8]  T. Soulimane,et al.  Structural Changes of Cytochrome c552 from Thermus thermophilus Adsorbed on Anionic and Hydrophobic Surfaces Probed by FTIR and 2D‐FTIR Spectroscopy , 2001, Chembiochem : a European journal of chemical biology.

[9]  H. M. Farrell,et al.  Secondary structural studies of bovine caseins: temperature dependence of β-casein structure as analyzed by circular dichroism and FTIR spectroscopy and correlation with micellization , 2001 .

[10]  J. Gillespie,et al.  The proteins of the keratin component of bird's beaks. , 1976, Australian Journal of Biological Sciences.

[11]  H. Mantsch,et al.  Membrane binding induces destabilization of cytochrome c structure. , 1991, Biochemistry.

[12]  H. Edwards,et al.  Fourier-transform Raman spectroscopy of mammalian and avian keratotic biopolymers. , 1997, Spectrochimica acta. Part A, Molecular and biomolecular spectroscopy.

[13]  S. Colinart,et al.  Fabrication processes of archaeological Egyptian blue and green pigments enlightened by Raman microscopy and scanning electron microscopy , 1999 .