Abstract
A Biophysical Comparison of Human Serum Albumin to be GlycatedIn VivoandIn VitroThe glycation process includes the arrangement of proteins with chemically reversible early glycation products, Schiff bases and Amadori adducts. These early products endure slow and complex rearrangements to create advanced glycation end-products (AGEs) that are involved in diabetic complications. Here, the biophysical characteristics ofin vitroglycated human serum albumin (HSA) are compared to those of HSA glycatedin vivo. The changes in the content of α-helices, AGE-specific fluorescence intensity, extent of lysine residue modification, and surface tension value and also the formation of Amadori products in HSA are similar in both conditions. It was observed, however, that arginine residues were modified only under physiological conditions (in vivo), while the same did not occurin vitro. This difference was related to the presence of 3-deoxyglucosone, a 1,2-dicarbonyl compound derived from glucose under physiological conditions. Therefore, the biophysical studies on the HSA glycation processin vitroare credible.
Highlights
Nonenzymatic protein glycation, as a multi-step chemical process, is the first event of hyperglycemia in biological fluids as well as tissues
These early products endure slow and complex rearrangements to create advanced glycation end-products (AGEs) that are involved in diabetic complications
The biophysical characteristics of in vitro glycated human serum albumin (HSA) are compared to those of HSA glycated in vivo
Summary
Nonenzymatic protein glycation, as a multi-step chemical process, is the first event of hyperglycemia in biological fluids as well as tissues. This process is pathophysiologically important in the etiology of the long-term complications of diabetes It involves the Address for correspondence: Naghmeh Sattarahmady Department of Biochemistry, Shiraz University of Medical Sciences, Shiraz, Iran Tel: +98 711 2303029, Fax: +98 711 2303029 e-mail: sattarahmadyayahoo.com reaction of glucose with a number of amino acid sidechains bearing nucleophilic groups (such as the e-amino groups of lysine residues and the N-terminal group of proteins). It yields a class of heterogeneous chemical compounds collectively referred to as advanced glycation end-products (AGE).
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