International Journal of Biological Macromolecules 2015-08-01

Zinc inhibits glycation induced structural, functional modifications in albumin and protects erythrocytes from glycated albumin toxicity.

Rashmi Tupe, Amruta Kulkarni, Krishna Adeshara, Neena Sankhe, Shamim Shaikh, Sayli Dalal, Siddharth Bhosale, Sushama Gaikwad

Index: Int. J. Biol. Macromol. 79 , 601-10, (2015)

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Abstract

The present work aims to investigate the concentration and time dependant effect of zinc on the in vitro non enzymatic modifications of albumin by diabetic levels of glucose. Further, preventive and curative effect of zinc was studied by adding zinc before and after initiation of glycation respectively. Glycation of albumin was done at different concentrations of zinc (125, 250 and 500 μM) at different time intervals (21, 28 and 35 days) with appropriate controls. The antiglycation potential of zinc was assessed by estimating different markers of albumin glycation (fructosamines, carbonyls, bound sugar, AGEs), structural modifications (free amino, thiol group, β amyloid, native PAGE, ANS binding, fluorescence lifetime decay and CD analysis) and functional properties (antioxidant activity, hemolysis). Zinc at highest concentration (500 μM) significantly reduced modifications of albumin which was comparable to aminoguanidine and also protected secondary and tertiary structure of albumin after 28 days of incubation. Zinc exhibited significant protective effect on erythrocytes by inhibiting hemolysis. Thus the present study indicate preventive mode of albumin glycation inhibition by zinc.Copyright © 2015 Elsevier B.V. All rights reserved.