Physico-Chemical Changes of Human Serum Albumin During in Vivo and in Vitro Glycation Processes

N. Sattarahmady(1*), A.A. Moosavi-Movahedi(2), M. Habibi-Rezaei(3), H. Heli(4)

(1) Department of Biochemistry, Shiraz University of Medical Sciences, Shiraz, Iran., Iran, Islamic Republic of
(2) Institute of Biochemistry and Biophysics, University of Tehran, Tehran, Iran., Iran, Islamic Republic of
(3) School of Biology, College of Sceince, University of Tehran, Tehran, Iran., Iran, Islamic Republic of
(4) Department of chemistry, Islamic Azad University, Fars Science and Research Branch, Marvdasht, Iran., Iran, Islamic Republic of
(*) Corresponding author

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Glycation, a post-translational modifications, 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 involved in diabetic complications. Here, physico-chamical characteristics of in vitro glycated human serum albumin (HSA) during 14 and 28 days incubation at the presence of glucose inquire with that happened in human serum. The formation of Amadori products, AGE-specific fluorescence intensity, extent of lysine residue modification and the changes in the content of α-helices, and also surface tension value in HSA are all in similar manners in both conditions. It was observed, however, that arginine residues were modified only under physiological conditions (in vivo), and did not occur in 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 process in vitro are credible
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Human Serum Albumin; Glycation; Diabetic Individual; Arginine Residue

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