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阿魏酸对不同单糖介导的牛血清白蛋白蛋白糖化和氧化损伤的比较研究。

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

机构信息

Program in Clinical Biochemistry and Molecular Medicine, Department of Clinical Chemistry, Faculty of Allied Health Sciences, Chulalongkorn University, Bangkok 10330, Thailand.

出版信息

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

DOI:10.3390/molecules181113886
PMID:24284487
原文链接:https://pmc.ncbi.nlm.nih.gov/articles/PMC6270180/
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.

摘要

三种膳食单糖(葡萄糖、果糖和核糖)的蛋白质糖化速率不同,这会加速晚期糖基化终产物(AGEs)的产生。本研究旨在探讨阿魏酸(FA)对三种单糖介导的蛋白质糖化和 BSA 氧化的影响。通过比较百分比的降低,FA(1-5 mM)降低了葡萄糖糖化 BSA 中的荧光 AGEs(F-AGEs)和 N(ε)-(羧甲基)赖氨酸(N(ε)-CML)的水平(F-AGEs = 12.61%-36.49%;N(ε)-CML = 33.61%-66.51%),果糖糖化 BSA(F-AGEs = 25.28%-56.42%;N(ε)-CML = 40.21%-62.91%)和核糖糖化 BSA(F-AGEs = 25.63%-51.18%;N(ε)-CML = 26.64%-64.08%)。此外,FA 降低果糖胺(Frc)和淀粉样交叉 β 结构(Amy)的百分比分别为 Frc = 20.45%-43.81%;Amy = 17.84%-34.54%在葡萄糖糖化 BSA 中,Frc = 25.17%-36.92%;Amy = 27.25%-39.51%在果糖糖化 BSA 中,以及 Frc = 17.34%-29.71%;Amy = 8.26%-59.92%在核糖糖化 BSA 中。FA 还诱导葡萄糖糖化 BSA 中蛋白质羰基含量(PC)和蛋白质巯基损失(TO)的降低(PC = 37.78%-56.03%;TO = 6.75%-13.41%),果糖糖化 BSA(PC = 36.72%-52.74%;TO = 6.18%-20.08%)和核糖糖化 BSA(PC = 25.58%-33.46%;TO = 20.50%-39.07%)。有趣的是,FA 降低荧光 AGEs 与 N(ε)-CML、果糖胺、淀粉样交叉 β 结构和蛋白质羰基含量的水平相关。因此,FA 可能具有抑制单糖引起的蛋白质糖化和氧化损伤的潜力,提示其可能预防糖尿病并发症期间 AGEs 介导的病理。

https://cdn.ncbi.nlm.nih.gov/pmc/blobs/2604/6270180/36c845f4803f/molecules-18-13886-g006.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/2604/6270180/9f892a40db57/molecules-18-13886-g001.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/2604/6270180/cdf2233cf351/molecules-18-13886-g002.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/2604/6270180/d38a35b8db1e/molecules-18-13886-g003.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/2604/6270180/148292e956c5/molecules-18-13886-g004.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/2604/6270180/e4b58f4c0a89/molecules-18-13886-g005.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/2604/6270180/36c845f4803f/molecules-18-13886-g006.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/2604/6270180/9f892a40db57/molecules-18-13886-g001.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/2604/6270180/cdf2233cf351/molecules-18-13886-g002.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/2604/6270180/d38a35b8db1e/molecules-18-13886-g003.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/2604/6270180/148292e956c5/molecules-18-13886-g004.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/2604/6270180/e4b58f4c0a89/molecules-18-13886-g005.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/2604/6270180/36c845f4803f/molecules-18-13886-g006.jpg

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