Amyloid-beta peptide-binding alcohol dehydrogenase (ABAD) inhibiting peptide, as 
a specific inhibitor between ABAD and amyloid-beta (Abeta), has been 
demonstrated to effectively inhibit Abeta peptide cytotoxicity. However, a major 
drawback is its short half-life, which results in the need for multiple 
applications and high synthesis costs. To overcome this, we established a 
lentiviral expression system that allowed the stable expression of the small 
ABAD-inhibiting peptide by fusion with cytosolic thioredoxin-1 (TRX). The fusion 
peptide, TA aptamer, was observed within PC12 cytoplasm and maintained both 
Abeta-binding ability and antioxygenic property similar to TRX. Our data showed 
that overexpression of both TRX and TA aptamer could protect PC12 cells from 
intracellular Abeta cytotoxicity. The present study suggests that TRX, as a 
cytosolic protein and a fusion motif, could not only assist ABAD-inhibiting 
peptide expression, cytoplasmic localization, but rebalance the disturbed "redox 
equilibrium" caused by intracellular Abeta in PC12 cells.