Table 1.
Diagnostic Peaks in Raman Spectra of Chondrocytes Used for the Analysis of Biochemical Changes
| Raman shift, cm−1 | Biochemical characteristic | References |
|---|---|---|
| 1004 | Symmetric ring breathing of phenylalanine | 77,78 |
| Absolute intensity of this peak is proportional to total protein in cells | 52,63,78,79 | |
| Collagen backbone C−C stretching | ||
| 854, 925 | Pro | 80 |
| 940 | C−C stretching mode of α-helical structure of collagen | 61 |
| 960–970 | Nonhelical telopeptide/less-ordered collagen | This work on the basis of Refs. 81,82 |
| 480 | Endocyclic (CCO, CCC) deformations; glycogen content | 83–86 |
| 1043–1050 | C−OH stretching mode of pyranose ring; polysaccharide content | 81,83 |
| 1300 | CH2 twisting mode of hydrocarbon chains; total lipids | 87 |
| 1657 | C=C stretching mode of unsaturated lipids (superimposed on the amide I peak of protein); total unsaturated lipids | 88 |
| ∼1750 | C=O stretching mode of ester groups of lipids | 88 |
| ∼790 | P−O stretching mode of phosphodiester (C5-O-P-O-C3) groups of DNA polysaccharide backbone structures; Total DNA | 77 |