Development of DNA Aptamer as a ß-Amyloid Aggregation Inhibitor.

ABSTRACT

Developing a strategy of modulating ß-amyloid (Aß) aggregation with low cost, easy synthesis, high efficiency, and biosafety is significant and a challenge for Alzheimer's disease (AD) therapy. Herein, DNA aptamer (Aß-Apt) against Aß42 obtained by in vitro selection was developed as a potent inhibitor of Aß42 aggregation for the first time. Indeed, the Aß42 monomer fibrillation was inhibited completely by Aß-Apt. Notably, the inhibition effect of Aß-Apt on the Aß42 oligomer aggregation was more obvious than that on the Aß42 monomer aggregation. It was presumed that the distinguishing effect may be attributed to different binding behaviors of Aß-Apt with Aß42 monomer and Aß42 oligomer. Surface plasmon resonance analysis demonstrated that Aß-Apt specifically recognized Aß42 monomer and Aß42 oligomer. Furthermore, the binding affinity of Aß-Apt with Aß42 oligomer was larger than that of Aß-Apt with Aß42 monomer. This work provided a promising platform with high efficiency for manipulating Aß aggregation.