The ageing of connective tissues involves modifications of collagen, w
hich are currently generating much interest amongst protein researcher
s. Protein glycation, a non-enzymic reaction involving sugar, appears
to play a role in the evolution of age-related physical changes and di
abetic complications-retinopathy, neuropathy, renal failure and athero
sclerosis. Our studies show that the glycation of human corneal and sc
leral collagen produces increases in the collagen intermolecular spaci
ng-these increases are similar to those we previously reported on the
ageing of collagen in these tissues. The present investigation employs
X-ray diffraction to look at the structural effects of various substa
nces that are believed in inhibit protein glycation. Aspirin-like comp
ounds and certain vitamins successfully prevented the sugar-induced mo
lecular changes from occurring in corneal and scleral collagen, sugges
ting that such compounds could have a useful role in this aspect of ag
eing.