Planta Med 2009; 75 - PD40
DOI: 10.1055/s-0029-1234519

Quercetin-3-rutinoside, a flavonol glycoside from Teucrium polium suppresses advanced glycation end products (AGEs) formation: A structural study

MA Esmaeili 1, H Sadeghi 2, N Karimian Pour 3
  • 1Department of Biology, Medicinal Plants and Drug Research Institute, Shahid Beheshti University, G.C. Tehran, Iran
  • 2Department of Biochemistry, School of Medicine, Yasuj University of Medical Sciences, Yasuj, Iran
  • 3Department of Biochemistry, the Hospital for Sick Children, University of Toronto, Toronto, ON M5G 1X8, Canada

In this study, isolation and structure elucidation of the high antioxidant and antiglycation compound(s) from Teucrium polium were performed. Based on our results, rutin (quercetin-3-rutinoside), a flavonol glycoside isolated from T. polium exhibited high antioxidant activity compared to the other isolated compounds from T. polium.

The protein glycation inhibitory activity of rutin was also evaluated in vivo using various models [1, 2, 3]. In the early stage of protein glycation rutin showed a moderately inhibitory activity on HbA1C formation, which were similar to that of aminoguanidine, a well-known inhibitor for advanced glycation endproducts (AGEs). For the middle stage, rutin developed more significant inhibitory effect on methylglyoxal-medicated protein modification, and in the last stage of glycation, rutin was found to be potent inhibitor of both the AGEs formation and the subsequent cross-linking of proteins. Furthermore, the effect of rutin on preventing oxidative protein damages including effect on protein carbonyl (PCO) formation and thiol oxidation which are believed to form under the glycoxidation process was achieved. Rutin inhibited high glucose induced oxidative damages to protein by decreasing PCO formation and preventing thiols group from oxidation. In addition, the structural changes of human serum albumin with glucose, in the presence of rutin were evaluated by circular dichroism and fluorescence techniques. Regarding enhancing the helicity of the protein and prevents helix decrement in the secondary structure of human serum albumin in the presence of glucose, it can be concluded that rutin may be act as an anti-glycation agent for human serum albumin.

Acknowledgements: This research work was supported by the Research Council of Shahid Beheshti University (G.C), Tehran, Iran. We also extend our thanks to Mrs. M. Ashorzadeh for her instrumental assistance.

References: [1]Rahbar, S. et al. (2000) Mol. Cell Biol. Res. Commun. 3:360–366.

[2] Lee, C. et al. (1998)J. Biol. Chem. 273:25272–25278.

[3] Nagarai, R.H. et al. (1996)J. Biol. Chem. 271:19338–19345.