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Abstract
A feature of diabetes is that the rate of protein glycation and the formation of advanced glycation endproducts (AGEs) increases spontaneously due to the abnormally elevated levels of sugar in the blood. The glycation of proteins is associated with a large number of late diabetic complications (retinopathy, neuropathy, atherosclerosis, end stage renal diseases, rheumatoid arthritis and neurodegenerative diseases). The increase in diabetic complications is a major cause of morbidity and mortality, which has increased significantly in the last two decades. Therefore, there is a considerable recent interest in the identification of lead molecules, which can inhibit the glycation process or slow it down considerably. A new class of anti-glycation agents has been identified, based on the spectrofluorimetric analysis of fluorescent advanced glycation endproducts (AGEs), benzenediol Schiff bases, and their structure-activity relationships have been studied. Some of these compounds have shown a promising anti-glycation potential in vitro.
Acknowledgements
We are grateful to the Umaer Basha Foundation (USA) for travel support and scholarship to Ghulam Abbas for his study visit to USA. We are thankful to Samina Abdul Sattar and Shahida Perveen for conducting the cytotoxicity assays. We are also grateful to Atia-tul-Wahab for her help in the preparation of this manuscript.
Declaration of interest
The author declare no conflict of interest.