| Abstract: | The inhibition of amyloid‐β (Aβ) aggregation has been regarded as the primary therapeutic strategy for Alzheimer's diseases (AD). Currently, many kinds of amyloid inhibitors have been explored, but these inhibitors have their own drawbacks. This study proposes and demonstrates a new kind of inhibitor in this work by making use of protease endowed with high selectivity to prevent Aβ aggregation. To do this, a nanoconjugate that is composed of chymotrypsin, Aβ aptamer, and gold nanoparticle is designed and fabricated. The nanoconjugate can actively capture Aβ through interaction between the aptamer and Aβ, and destroy the target peptides through proteolysis mediated by the adjacent protease molecules. Compared with the conventional inhibitors that only passively bind with Aβ, this new kind of inhibitor may provide a novel insight to control Aβ aggregation. The multivalent binding and efficient enzymatic reaction toward Aβ may also enable a more complete clearance of Aβ, which might achieve a better treatment effect for AD in the future. |
