Spectroscopy and Molecular Changes in Cancer Cells - Vibrational Spectroscopy for Tissue Analysis - page 27

840-860 cm −1 has been assigned to polysaccharides, 1420-1450 cm −1
to CH 2 scissoring vibrations in lipids, and 928-940 cm −1 to ν(C- C)
stretching in amino acids proline and valine.

Frank et al. [34] presented a detailed database for collagen peak intensities
in normal and cancerous human breast tissue. These intensities are tabulated
in Table 2.3. According to these results, collagen has 14 peak intensities, and
cancer will cause some changes in the position of these peaks. Almost all of
these peaks have been used in human skin samples by Cheng et al. [35].
Pichardo-Molina et al. studied serum samples using Raman spectroscopy
and different statistical methods [36]. The blood samples were obtained from
11 patients who were clinically diagnosed with breast cancer and 12 healthy
volunteer controls. The wavelength differences between the spectral bands
of the control and patient groups were defined. It was shown that serum
samples from patients with breast cancer and from the control group can be
discriminated using Raman spectroscopy. It was also found that seven band
ratios were significant in the diagnosis process. These specific bands might
be helpful during screening for breast cancer using Raman spectroscopy of
serum samples. The group presented a detailed table documenting all the
spectral information observed in the two groups of samples. It is illustrated
that there are considerable spectral differences between the peak intensities
of control samples and those of cancerous blood serum (Table 2.4).

Table 2.3
Collagen Assignments in Human Breast Tissue (34)

Peak Position in
Normal Tissue (cm −1 )

Peak Position in Infiltrating
Ductal Carcinoma (cm −1 ) Collagen Assignment

- 817 C-C stretch

727 856 C-C stretch, proline

870 876 C-C stretch, hydroxyproline

- 920 C-C proline ring

972 937 C-C backbone

- 1004 Phenylalanine

1066 1043 Proline

- 1206 Hydroxyproline, tyrosine

- 1247 Amide III

1265 1267 Amide III

1303 1303 CH 3 CH 2 twisting

- 1343 CH 3 CH 2 wagging

1439 1450 CH 3 CH 2 deformation

1654 1657 Amide I

Source: C. J. Frank, R. L. McCreecy, and D. C. B. Redd. Raman spectroscopy of normal
and diseased human breast tissues. Anal. Chem . 67(1995): 777-783. With
permission.