Alteration of the thermodynamic characteristics of corneal collagen denaturation as a result of nonenzymatic glycation

Moscow University Chemistry Bulletin - Tập 62 - Trang 63-66 - 2007
N. Yu. Ignati’eva1, N. A. Danilov1, V. V. Lunin1, M. V. Obrezkova1, S. V. Averkiev1, T. I. Chaikovskii1
1Physical Chemistry Department, Russia

Tóm tắt

The thermal stability of the scleral and corneal tissues after in vitro treatment with ribose, threose, and glyceraldehyde was investigated. The thermal transition temperature and the enthalpy of collagen fiber crosslinking were determined by differential scanning calorimetry (DSC). The resistance of the tissues toward trypsin was also determined after heating tissue samples in the DSC furnace. It was shown that the denaturation temperature of scleral and corneal samples treated by crosslinking agents increased, but the enthalpy of denaturation decreased. It is suggested that crosslinking in the collagen matrix of the cornea and sclera prevents complete collagen denaturation if the temperature does not rise up to 110 °C.

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Moscow University Chemistry Bulletin

Tập 62

63-66

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