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Molecules 2013, 18(11), 13886-13903; doi:10.3390/molecules181113886
Article

A Comparative Study of Ferulic Acid on Different Monosaccharide-Mediated Protein Glycation and Oxidative Damage in Bovine Serum Albumin

1
, 1
, 2
 and 3,4,*
1 Program in Clinical Biochemistry and Molecular Medicine, Department of Clinical Chemistry, Faculty of Allied Health Sciences, Chulalongkorn University, Bangkok 10330, Thailand 2 Department of Comparative Biomedical Sciences, School of Veterinary Medicine, Louisiana State University, Baton Rouge, LA 70803, USA 3 Research Group of Herbal Medicine for Prevention and Therapeutic of Metabolic Diseases, Chulalongkorn University, Bangkok 10330, Thailand 4 The Medical Food Research and Development Center, Department of Nutrition and Dietetics, Faculty of Allied Health Sciences, Chulalongkorn University, Bangkok 10330, Thailand
* Author to whom correspondence should be addressed.
Received: 9 October 2013 / Revised: 4 November 2013 / Accepted: 6 November 2013 / Published: 11 November 2013
(This article belongs to the Section Medicinal Chemistry)
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Abstract

Three dietary monosaccharides, (glucose, fructose, and ribose), have different rates of protein glycation that accelerates the production of advanced glycation end-products (AGEs). The present work was conducted to investigate the effect of ferulic acid (FA) on the three monosaccharide-mediated protein glycations and oxidation of BSA. Comparing the percentage reduction, FA (1–5 mM) reduced the level of fluorescence AGEs (F-AGEs) and Nε-(carboxymethyl) lysine (Nε-CML) in glucose-glycated BSA (F-AGEs = 12.61%–36.49%; Nε-CML = 33.61%–66.51%), fructose-glycated BSA (F-AGEs = 25.28%–56.42%; Nε-CML = 40.21%–62.91%), and ribose-glycated BSA (F-AGEs = 25.63%–51.18%; Nε-CML = 26.64%–64.08%). In addition, the percentages of FA reduction of fructosamine (Frc) and amyloid cross β-structure (Amy) were Frc = 20.45%–43.81%; Amy = 17.84%–34.54% in glucose-glycated BSA, Frc = 25.17%–36.92%; Amy = 27.25%–39.51% in fructose-glycated BSA, and Frc = 17.34%–29.71%; Amy = 8.26%–59.92% in ribose-glycated BSA. FA also induced a reduction in protein carbonyl content (PC) and loss of protein thiol groups (TO) in glucose-glycated BSA (PC = 37.78%–56.03%; TO = 6.75%–13.41%), fructose-glycated BSA (PC = 36.72%–52.74%; TO = 6.18%–20.08%), and ribose-glycated BSA (PC = 25.58%–33.46%; TO = 20.50%–39.07%). Interestingly, the decrease in fluorescence AGEs by FA correlated with the level of Nε-CML, fructosamine, amyloid cross β-structure, and protein carbonyl content. Therefore, FA could potentially be used to inhibit protein glycation and oxidative damage caused by monosaccharides, suggesting that it might prevent AGEs-mediated pathologies during diabetic complications.
Keywords: protein glycation; oxidative damage; ferulic acid; monosaccharides; advanced glycation end-products (AGEs); comparative study protein glycation; oxidative damage; ferulic acid; monosaccharides; advanced glycation end-products (AGEs); comparative study
This is an open access article distributed under the Creative Commons Attribution License which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited.

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MDPI and ACS Style

Sompong, W.; Meeprom, A.; Cheng, H.; Adisakwattana, S. A Comparative Study of Ferulic Acid on Different Monosaccharide-Mediated Protein Glycation and Oxidative Damage in Bovine Serum Albumin. Molecules 2013, 18, 13886-13903.

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