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Molecules. 2013 Nov 11;18(11):13886-903. doi: 10.3390/molecules181113886.

A comparative study of ferulic acid on different monosaccharide-mediated protein glycation and oxidative damage in bovine serum albumin.

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1
Program in Clinical Biochemistry and Molecular Medicine, Department of Clinical Chemistry, Faculty of Allied Health Sciences, Chulalongkorn University, Bangkok 10330, Thailand. sirichai.a@chula.ac.th.

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 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.

PMID:
24284487
DOI:
10.3390/molecules181113886
[Indexed for MEDLINE]
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