Influence of in vitro non-enzymatic glycosylation on the physicochemical parameters of type I collagen.
In vitro non-enzymatic condensation of glucose on acid soluble collagen is shown not to affect the molecular structure and stability as evaluated both by circular dichroism and differential spectrometry. Viscometric studies demonstrate a lowering in intermolecular interactions; whereas the hydrodynamic volume remains unaffected by nonenzymatic glycosylation. alpha 2(I) collagen chains exhibit a modified electrophoretic mobility previously found in collagen of diabetic rats; this peculiar behavior is discussed in terms of lowered hydrophobicity due to addition of hydrophilic groups from glucose. The lowered formation of hydrophobic areas, evaluated from the fluorescence emission of diphenylhexatriene, indicates that non-enzymatic glycosylation is able to influence the close packing of collagen fibers.
D000818:Animals; D055598:Chemical Phenomena; D002627:Chemistry, Physical; D002942:Circular Dichroism; D003094:Collagen / Q000032:analysis*; D004548:Elasticity; D006358:Hot Temperature; D007525:Isoelectric Focusing; D011489:Protein Denaturation; D051381:Rats; D013997:Time Factors; D014783:Viscosity
D003094:Collagen