Dihydroxyacetone disturbs collagen fibril formation due to side chain modifications by glycation (979.1)

Glycation is a spontaneous process typically initiated with a condensation reaction between a reducing sugar and a protein, leading to the formation of Advanced Glycation Endproducts (AGEs). The in vivo accumulation of AGEs has been shown to modify the side chains of long lived proteins such as collagen, resulting in the alteration of their functions. The objective of this study was to use a combination of analytical techniques to evaluate the effect of dihydroxyacetone (DHA), an FDA approved tanning agent, on collagen glycation and fibril formation. Fluorescence spectroscopy revealed that DHA readily glycated collagen and induced the formation of AGEs. Moreover, addition of DHA to a collagen solution disturbed fibril formation, an observation confirmed by both UV spectroscopy and transmission electron microscopy (TEM). Compared to control solutions with collagen alone, addition of DHA showed a similar extent of fibril formation, but with a much lower rate, suggesting a reversible association of DHA which...