Controversial behavior of aminoguanidine in the presence of either reducing sugars or soluble glycated bovine serum albumin |
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Authors: | Serban Andreea Iren Costache Marieta Dinischiotu Anca |
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Institution: | aUniversity of Agricultural Science and Veterinary Medicine, Faculty of Veterinary Medicine, 105 Splaiul Independentei 050097, Bucharest 5, Romania;bUniversity of Bucharest, Faculty of Biology, Molecular Biology Center, 91-95 Splaiul Independentei 050089, Bucharest 5, Romania |
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Abstract: | The elucidation of the controversial inhibitory effect of aminoguanidine (AG) on the cross-linking and fluorescent advanced glycation end products (AGEs) formation during long-term in vitro glycation of type I collagen with 250 mM reducing sugars or 0.5 mg/ml soluble glycated bovine serum albumin (AGE-BSA) was researched.Chromatographic and SDS–PAGE analyses revealed the formation of aggregates during collagen glycation. AG at all concentrations (5–80 mM) prevented the cross-linking of collagen peptides with monosaccharides but an increase in fluorescence with a maximum value at 10 mM AG was noticed. In the presence of AGE-BSA, AG prevented the cross-linking process and decreased the fluorescence levels in a concentration-dependent manner.Our results suggest that AG is an efficient inhibitor of collagen cross-linking and the highest increase in fluorescence due to reducing sugars and AG can be explained by the competition between guanidine group of AG and arginine residues of some protein-bound dideoxyosones, which could form fluorescent compounds. |
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Keywords: | Advanced glycation end products (AGEs) Glucose Ribose Aminoguanidine Collagen Fluorescence |
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