Journal of Enzyme Inhibition and Medicinal Chemistry · 2010 · 20 citations · 20 references
Life SciencesBiochemistryPharmacologyDrug DiscoveryGlycobiologyStructure-activity RelationshipsDiabetes Mellitus BiochemistryEnzyme InhibitionProtein GlycosylationAdvanced Glycation End ProductsChemical Structure-activity RelationshipsDiabetic ComplicationsLate ComplicationsProtein Glycoxidation
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.
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Pharmacological Inhibition of Diabetic Retinopathy
Timothy S. Kern, Ronald L. Engerman · Diabetes · 2001 · 276 citations · Full text