The increased erythrocyte aggregation observed in diabetes mellitus is
mainly due to changes in the balance between aggregating factors and
anti-aggregating ones, like albumin. Since chronic hyperglycaemia resu
lts in protein glycation, we examined the effect of in vitro glycation
of albumin on its anti-aggregating role with blood from 29 Type 1 dia
betic patients and 29 healthy controls. After the addition of glycated
and unglycated albumin, samples had a glycation level of 24 % for hea
lthy controls and 28 % for diabetic patients. Erythrocyte aggregation
was determined by the analysis of the light backscattered by a blood s
uspension. Erythrocytes from healthy controls suspended in glycated al
bumin had significantly higher rates of rouleaux formation (p < 0.01)
than in unglycated albumin and increased cohesion of rouleaux (p < 0.0
5). The erythrocyte aggregation in diabetic patients underwent similar
changes (p < 0.01). The time-resolved fluorescence of the single tryp
tophan residue was monitored to describe the changes in the conformati
onal equilibrium of albumin. The lifetime data showed that the increas
es in the two lifetime components and in the relative proportion of th
e major lifetime are in agreement with a conformational change in albu
min after glycation. Thus, the changes in albumin conformation could b
e responsible for the smaller hypoaggregating effect of glycated album
in.