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

Molecules

Weerachat Sompong¹  Aramsri Meeprom¹  Henrique Cheng² 

[1] Program in Clinical Biochemistry and Molecular Medicine, Department of Clinical Chemistry, Faculty of Allied Health Sciences, Chulalongkorn University, Bangkok 10330, Thailand; E-Mails:;Department of Comparative Biomedical Sciences, School of Veterinary Medicine, Louisiana State University, Baton Rouge, LA 70803, USA; E-Mail:

关键词: protein glycation;    oxidative damage;    ferulic acid;    monosaccharides;    advanced glycation end-products (AGEs);    comparative study;   

DOI  :  10.3390/molecules181113886

来源: mdpi

【 摘 要 】

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 N^ε-(carboxymethyl) lysine (N^ε-CML) in glucose-glycated BSA (F-AGEs = 12.61%–36.49%; N^ε-CML = 33.61%–66.51%), fructose-glycated BSA (F-AGEs = 25.28%–56.42%; N^ε-CML = 40.21%–62.91%), and ribose-glycated BSA (F-AGEs = 25.63%–51.18%; N^ε-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 N^ε-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.

【 授权许可】

CC BY   
© 2013 by the authors; licensee MDPI, Basel, Switzerland.