Department of Biotechnology, Barkatullah University, Bhopal (M.P.) 462026
Department of Pharmacology, Gandhi Medical College, Bhopal (M.P.) 462026
Department of Chemistry, MLB, Girl (PG) College, Bhopal (M.P.) 462026
Various diabetes complications are due to protein glycation and the formation of advanced glycation end products. When AGEs accumulations particularly high in E.C.M., proteins are result in intra and inter molecular cross-linking and later has been hypotized to stiffening of these proteins and believed to play an important role in etiology of various AGEs related diseases. The anti-glycation activity of W. somnifera phytoconstituents which target the essential stages of glycation through-(i) inhibition (ii) reduction of AGEs cross- linking. The inhibitory and Crosslink breaker activity of root and leaf extracts of W. somnifera showedthe best results obtained by colorimetric methods selected for molecular level. The peak width of native protein collagen/elastin (0.114, 0.102Wi) was compared with glycated (0.215, 0.198 Wi) at inflation points and significant difference were observed. The peak width was the indication of shape of the protein and clearly distinguishes the results of inhibition as well as crosslink breaking activity, which is helpful in prophylaxis of aging, overall diabetes management strategy and also reduced the risk of AGEs related disease (retinopathy, neuropathy, nephropathy).
Key words:- non-enzymatic glycation , inhibition , nitroblue tetrazolium reduction assay , diabetic complication ,