Abstract: Cinnamic acid and its derivatives have shown a variety of pharmacologic properties. However, little is known about the antiglycation properties of cinnamic acid and its derivatives. The present study sought to characterize the protein glycation inhibitory activity of cinnamic acid and its derivatives in a bovine serum albumin (BSA)/fructose system. The results demonstrated that cinnamic acid and its derivatives significantly inhibited the formation of advanced glycation end products (AGEs) by approximately 11.96–63.36% at a concentration of 1 mM. The strongest inhibitory activity against the formation of AGEs was shown by cinnamic acid. Furthermore, cinnamic acid and its derivatives reduced the level of fructosamine, the formation of Nε-(carboxymethyl) lysine (CML), and the level of amyloid cross β-structure. Cinnamic acid and its derivatives also prevented oxidative protein damages, including effects on protein carbonyl formation and thiol oxidation of BSA. Our findings may lead to the possibility of using cinnamic acid and its derivatives for preventing AGE-mediated diabetic complications.
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Adisakwattana, S.; Sompong, W.; Meeprom, A.; Ngamukote, S.; Yibchok-anun, S. Cinnamic Acid and Its Derivatives Inhibit Fructose-Mediated Protein Glycation. Int. J. Mol. Sci. 2012, 13, 1778-1789.
Adisakwattana S, Sompong W, Meeprom A, Ngamukote S, Yibchok-anun S. Cinnamic Acid and Its Derivatives Inhibit Fructose-Mediated Protein Glycation. International Journal of Molecular Sciences. 2012; 13(2):1778-1789.
Adisakwattana, Sirichai; Sompong, Weerachat; Meeprom, Aramsri; Ngamukote, Sathaporn; Yibchok-anun, Sirintorn. 2012. "Cinnamic Acid and Its Derivatives Inhibit Fructose-Mediated Protein Glycation." Int. J. Mol. Sci. 13, no. 2: 1778-1789.