Abstract
This manuscript describes the protein anti-glycation activity of thirty-three (33) benzothiazoles, out of which twenty-seven were the newly synthesized benzothiazoles. Compound 1 (IC50= 187 ± 2.6 µM) was found to be the most active, while compounds 2 (IC50= 219 ± 3.6 µM), 3 (IC50= 224 ± 1.9 µM), 4 (IC50= 223 ± 3.3 µM), 5 (IC50= 238 ± 2.2 µM), 7 (IC50= 266 ± 5.4 µM), 17 (IC50= 226 ± 1.6 µM) and 18 (IC50= 274 ± 2.4 µM) were significantly active, when compared with the standard rutin (IC50= 294 ± 1.5 µM). This study identified potential inhibitors of methylglyoxal mediated glycation of proteins, which is the pathophysiology of late diabetic complications.
Publication types
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Research Support, Non-U.S. Gov't
MeSH terms
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3T3 Cells
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Animals
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Benzothiazoles / chemical synthesis*
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Benzothiazoles / chemistry
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Benzothiazoles / pharmacology
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Cattle
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Cell Survival / drug effects
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Chickens
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Glycation End Products, Advanced / antagonists & inhibitors*
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Glycation End Products, Advanced / chemistry
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Glycosylation / drug effects
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Mice
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Muramidase / antagonists & inhibitors
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Muramidase / chemistry
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Pyruvaldehyde / chemistry*
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Rutin / pharmacology
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Serum Albumin, Bovine / antagonists & inhibitors
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Serum Albumin, Bovine / chemistry
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Structure-Activity Relationship
Substances
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Benzothiazoles
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Glycation End Products, Advanced
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Serum Albumin, Bovine
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Rutin
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Pyruvaldehyde
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Muramidase