The novel amyloid-beta peptide aptamer inhibits intracellular amyloid-beta peptide toxicity

被引：0

作者：

Xu Wang ^{[1
]}

Yi Yang ^{[1
]}

Mingyue Jia ^{[1
]}

Chi Ma ^{[2
]}

Mingyu Wang ^{[1
]}

Lihe Che ^{[3
]}

Yu Yang ^{[1
]}

Jiang Wu ^{[1
]}

机构：

[1] Department of Neurology, First Hospital of Jilin University

[2] Department of Neurosurgery, First Hospital of Jilin University

[3] Department of Infection, First Hospital of Jilin University

来源：

Neural Regeneration Research | 2013年 / 8卷 / 01期

基金：

中国国家自然科学基金;

关键词：

neural regeneration; neurodegenerative disease; gene therapy; Alzheimer’s disease; aptamer; amyloid; β; peptide; amyloid β peptide binding alcohol dehydrogenase; decoy peptide; thioredoxin; mitochondrial dysfunction; molecular cloning; grants-supported paper; photographs-containing paper; neuroregeneration;

D O I：

暂无

中图分类号：

R749.1 [脑器质性精神障碍];

学科分类号：

100205 ;

摘要：

Amyloid β peptide binding alcohol dehydrogenase (ABAD) decoy peptide (DP) can competitively antagonize binding of amyloid β peptide to ABAD and inhibit the cytotoxic effects of amyloid β peptide. Based on peptide aptamers, the present study inserted ABAD-DP into the disulfide bond of human thioredoxin (TRX) using molecular cloning technique to construct a fusion gene that can express the TRX1-ABAD-DP-TRX2 aptamer. Moreover, adeno-associated virus was used to allow its stable expression. Immunofluorescent staining revealed the co-expression of the transduced fusion gene TRX1-ABAD-DP-TRX2 and amyloid β peptide in NIH-3T3 cells, indicating that the TRX1-ABAD-DP-TRX2 aptamer can bind amyloid β peptide within cells. In addition, cell morphology and MTT results suggested that TRX1-ABAD-DP-TRX2 attenuated amyloid β peptide-induced SH-SY5Y cell injury and improved cell viability. These findings confirmed the possibility of constructing TRX-based peptide aptamer using ABAD-DP. Moreover, TRX1-ABAD-DP-TRX2 inhibited the cytotoxic effect of amyloid β peptide.

引用

页码：39 / 48

页数：10

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