Neural Regeneration Research ›› 2013, Vol. 8 ›› Issue (1): 39-48.doi: 10.3969/j.issn.1673-5374.2013.01.005

Previous Articles     Next Articles

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

Xu Wang1, Yi Yang1, Mingyue Jia1, Chi Ma2, Mingyu Wang1, Lihe Che3, Yu Yang1, Jiang Wu1   

  1. 1 Department of Neurology, First Hospital of Jilin University, Changchun 130021, Jilin Province, China
    2 Department of Neurosurgery, First Hospital of Jilin University, Changchun 130021, Jilin Province, China
    3 Department of Infection, First Hospital of Jilin University, Changchun 130021, Jilin Province, China
  • Received:2012-09-08 Revised:2012-11-07 Online:2013-01-05 Published:2013-01-05
  • Contact: Jiang Wu, M.D., Ph.D., Professor, Department of Neurology, First Hospital of Jilin University, Changchun 130021, Jilin Province, China, sjnkwujiang@sina.com.cn. Yu Yang, M.D., Ph.D., Associate professor, Department of Neurology, First Hospital of Jilin University, Changchun 130021, Jilin Province, China, yy197711@yahoo.com.cn.
  • About author:Xu Wang☆, Studying for doctorate.
  • Supported by:

    This study was supported by the National Natural Science Foundation of China, No. 30872721; the National Natural Science Foundation for the Youth, No. 30801211, 30800338; and the Scientific Research Foundation for New Teachers of High Institutes, No. 200801831073, 200801831072.

PDF

1732

Abstract:

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.

Key words: neural regeneration, neurodegenerative disease, gene therapy, Alzheimer’s disease, aptamer, amyloid &beta, peptide, amyloid &beta, peptide binding alcohol dehydrogenase, decoy peptide, thioredoxin, mitochondrial dysfunction, molecular cloning, grants-supported paper, photographs-containing paper, neuroregeneration