Structure and conformation of intramolecularly cross-linked collagen.

This work reports the effects of cross-linking agent like formaldehyde (HCHO) and glutaraldehyde (GA) on monomeric collagen and its conformational stability using circular dichroism. The nature of the bonds formed and the stability of the cross-links introduced vary with the aldehyde. The amount of HCHO required is four times greater than GA to induce similar changes in the molar ellipticity. This is due to the structural changes of collagen-aldehyde reaction. The change in the molar ellipticity and Rpn ratio for HCHO and GA treated collagen suggest possible aggregation of collagen molecule. The relative viscosity of native and aldehyde treated collagen was measured and correlated to the changes seen in the CD spectra. The small amount of aldehydes are needed to induce changes in the conformational stability of collagen. This can be applied to the biomaterial and biomedical application.