Infrared and Raman Spectroscopy and Imaging of Breast Cancer - Vibrational Spectroscopy for Tissue Analysis - page 115

Table 5.2
Peak Assignments of the Raman Spectra of Breast Tissue [18]

Peak Assignment Normal DCIS HNG DCIS ING DCIS LNG IDC GI IDC GII IDC GIII

3300-2800 cm -1 ( C-H stretching vibrations of methyl ( CH 3 ) and methylene ( CH 2 ) groups of phospholipids, cholesterol and creatine 46,60 )
CH 3 (ν a s CH 3 of lipids, DNA, and proteins 32 )

2959 2958 2958 2957 2959 2957 2957

CH 2 (ν a s CH 2 of lipids 24,32,38 ) 2930 2930 2930 2930 2930 2930 2930

2884 2882 2881 2880 2882 2880 2880

CH 2 (ν s CH 2 of lipids 24,32,38 ) 2851 2851 2850 2850 2849 2849 2849

Vibrational bands for lipids, proteins, collagen, etc. 1670-750 cm -1
C = C (amide I (C = O stretching mode of proteins, α-helix
conformation)/C = C lipid stretch 44 )

1662 1660 1658 1658 1660 1659 1658

CH 2 (overlapping asymmetric CH 3 bending & CH 2
scissoring (is associated with elastin, collagen &
phospholipids) 29,30,61 )

1442 1452 1452 1451 1452 1452 1452

1260 1261 1261 1260 1261 1260 1260

C-N-H (ν(CN), δ(NH) amide III, α-helix conformation
collagen, tryptophan; and PO 2 - asymmetric
(Phosphate I) 38,39,41 )

O-P-O (stretching PO 2 - symmetric (Phosphate II) of
phosphodiesters 31,38,62,63 )

1096 1096 1095 1095 1095 1095 1095

C-C (ν s (C-C), Symmetric ring breathing of phenylalanine
(protein assignment) band 39 )

- 992 992 992 992 992 992

C-C (C-C stretch or proline, hydroxyproline and tyrosine
and ν 2 PO 2 - stretch of nucleic acids bands 39,41,58 )

780 795 795 795 792 792 792

C-C (Symmetric breathing of tryptophan -
protein assignment 39,41,44 )

650 751 750 - - - -

540

Source: S. Rehman, Z. Movasaghi, A. T. Tucker, S. P. Joel, J. A. Darr, A. V. Ruban, and I. U. Rehman. Raman spectroscopic analysis of breast cancer tissues:

Identifying differences between normal, invasive ductal carcinoma and ductal carcinoma in situ of the breast tissue. Journal of Raman Spectroscopy
38(2007): 1345-1351. With permission.