Abstract
A systematic study of changes in the physicochemical characteristics of scleral collagen in the course of glycosylation by threose, including their dependence on the time changes of transverse cross-linking, was performed. Glycosylation by threose leads to a significant increase in heat, proteolytic, and biomechanical stability of collagen in the scleral tissue and has been shown to be a useful approach for stabilizing scleral collagen. It was found that a fraction of collagen with a reduced denaturation temperature is, apparently, an intermediate in the reaction of glycosylation by threose. The most likely reason for its occurrence is the elongation of the side chains of amino acid residues of the protein in the early stages.
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