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 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; in revised form: 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

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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.

AMA 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(11):13886-13903.

Chicago/Turabian Style

Sompong, Weerachat; Meeprom, Aramsri; Cheng, Henrique; Adisakwattana, Sirichai. 2013. "A Comparative Study of Ferulic Acid on Different Monosaccharide-Mediated Protein Glycation and Oxidative Damage in Bovine Serum Albumin." Molecules 18, no. 11: 13886-13903.

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