Advanced glycation endproducts (AGE) formation by glyceraldehyde with human serum albumin and human fibrinogen
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Sumário do trabalho- Introduction
- Materials and methods
- Results
ResumoGlycation and accumulation of advanced glycation endproducts (AGE) contribute to protein modification during normal aging and diabetes. Besides glucose and fructose, metabolites from both metabolic pathways are able to cause chemical modifications in tissue proteins. In the present sudy, human fibrinogen (hFib) and human serum albumin (hSA) were glycated in vitro with glyceraldehyde (GA) under physiological conditions. Structural and conformational changes of both proteins are observed in less than 24 hours. AGE formation was monitored by UV-visible and fluorescence spectroscopy. Fluorescence of native proteins at 342 nm (excitation 290 nm) decreases significantly with glycation time with a corresponding appearance of a new fluorescence peak at around 420 nm (excitation 340 nm) and at 440 nm (excitation 370 nm). In the UV spectrum, the endogenous protein peak increased with glycation and broadened when compared with non- glycated controls. Higher molecular weight bands in SDS-PAGE were observed after 2 hours incubation, suggesting protein crosslinking. The rate of AGE formation with the triose GA was estimated to increase 5,000 fold compared to glucose. Pseudo-first order rate constants for the decreasing of the tryptophane fluorescence peak and for the appearance of new fluorophore in solution were determined for the reaction of GA with hFib and hSA separately. This is the first report of comparison of GA glycation and AGE formation with hFib and hSA.
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