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异阿魏酸,一种新型的抗糖基化试剂,可抑制体外果糖和葡萄糖介导的蛋白质糖基化。

Isoferulic acid, a new anti-glycation agent, inhibits fructose- and glucose-mediated protein glycation in vitro.

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 May 30;18(6):6439-54. doi: 10.3390/molecules18066439.

DOI:10.3390/molecules18066439
PMID:23722732
原文链接:https://pmc.ncbi.nlm.nih.gov/articles/PMC6270372/
Abstract

The inhibitory activity of isoferulic acid (IFA) on fructose- and glucose-mediated protein glycation and oxidation of bovine serum albumin (BSA) was investigated. Our data showed that IFA (1.25-5 mM) inhibited the formation of fluorescent advanced glycation end products (AGEs) and non-fluorescent AGE [Nε-(carboxymethyl) lysine: CML], as well as the level of fructosamine. IFA also prevented protein oxidation of BSA indicated by decreasing protein carbonyl formation and protein thiol modification. Furthermore, IFA suppressed the formation of β-cross amyloid structures of BSA. Therefore, IFA might be a new promising anti-glycation agent for the prevention of diabetic complications via inhibition of AGEs formation and oxidation-dependent protein damage.

摘要

异阿魏酸(IFA)对果糖和葡萄糖介导的牛血清白蛋白(BSA)糖化和氧化的抑制活性进行了研究。我们的数据表明,IFA(1.25-5 mM)抑制了荧光晚期糖基化终产物(AGEs)和非荧光 AGE[Nε-(羧甲基)赖氨酸:CML]的形成,以及果糖胺的水平。IFA 还通过减少蛋白质羰基形成和蛋白质巯基修饰来防止 BSA 的蛋白质氧化。此外,IFA 抑制了 BSA 的β-交叉淀粉样结构的形成。因此,IFA 可能是一种新的有前途的抗糖化剂,可通过抑制 AGEs 的形成和氧化依赖性蛋白质损伤来预防糖尿病并发症。

https://cdn.ncbi.nlm.nih.gov/pmc/blobs/cf4e/6270372/72c351075689/molecules-18-06439-g007.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/cf4e/6270372/0f863baacd1c/molecules-18-06439-g001.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/cf4e/6270372/53f7e70b2038/molecules-18-06439-g002.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/cf4e/6270372/ba71bdc19b86/molecules-18-06439-g003.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/cf4e/6270372/44d08d942872/molecules-18-06439-g004.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/cf4e/6270372/f2158e34537b/molecules-18-06439-g005.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/cf4e/6270372/571c747acf8a/molecules-18-06439-g006.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/cf4e/6270372/72c351075689/molecules-18-06439-g007.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/cf4e/6270372/0f863baacd1c/molecules-18-06439-g001.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/cf4e/6270372/53f7e70b2038/molecules-18-06439-g002.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/cf4e/6270372/ba71bdc19b86/molecules-18-06439-g003.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/cf4e/6270372/44d08d942872/molecules-18-06439-g004.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/cf4e/6270372/f2158e34537b/molecules-18-06439-g005.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/cf4e/6270372/571c747acf8a/molecules-18-06439-g006.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/cf4e/6270372/72c351075689/molecules-18-06439-g007.jpg

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