Biomedical Engineering Reference
In-Depth Information
Fig. 11.2. Representative Raman spectra in the fingerprint region of human tooth
enamel and dentin. Peak assignments are marked
Table 11.1. Raman spectral peak assignments of human tooth enamel and dentin
Peak (cm 1 )
Assignment
959
ν 1 symmetric stretching mode of PO 4
431, 446
ν 2 symmetric bending mode of PO 4
1023, 1043, 1052, 1069
ν 3 asymmetric stretching mode of PO 4
579, 590, 608, 614
ν 4 asymmetric bending mode of PO 4
1104
ν 1 symmetric stretching mode of type A CO 3
1069
ν 1 symmetric stretching mode of type B CO 3
1242
Amide III (N-H)
1450
C-H bending mode
1665
Amide I (C=O)
asymmetric stretching mode and the
ν 4 asymmetric bending vibrations (see
Table 11.1 for peak positions). Mixed in with the
ν 1 symmetric
stretching mode of type B CO 3 2 . The enamel spectrum does not show sig-
nificant peaks from other moieties aside from apatite. The spectrum of dentin
on the other hand, along with peaks from carbonated hydroxyapatite, con-
tains several additional bands that can be assigned to be characteristic of the
protein collagen. These spectra correlate well with the different biochemical
compositions of these tissue types, suggesting that Raman spectroscopy is well
suited for studying dental hard tissues.
ν 2 mode is the
 
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