Using Raman spectroscopy we obtained the molecular information on the collagen hydrogels cross-linked with different reagents. Hydrogels were incubated with glyceraldehyde and 1-Ethyl-3-(3-dimethylaminopropyl) carbodiimide (EDC). In the glyceraldehyde-treated collagen hydrogels spectrum, the appearance of a new band at 935 cm-1 and increased intensity of the band at 1245 cm-1 which correspond to the C-C stretching mode of protein backbone and Amide III respectively indicated the change of packing of collagen molecules. Moreover, the elevated intensity of the band at 1452 cm-1 suggested a change in the motion of the lysine Ch2 groups. This can be explained by the cross-linking reaction occurring between the glyceraldehyde and lysine. In the EDC-treated collagen hydrogels spectrum, the band at 935 cm-1 also appeared; however, the intensity at 1245 cm-1 remained. This observation suggested that EDC modifies the secondary structure of collagen molecules within hydrogels to lesser extent compared to glyceraldehyde.

Raman spectroscopy detects non-enzymatically induced cross-links within collagen hydrogels

243rd National Meeting (2012)

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