Abstract
Alzheimer's disease (AD) is associated with the aggregation of the amyloid-beta (Aβ) peptides into toxic aggregates. How to inhibit the aggregation of Aβ peptides has been extensively studied over recent decades. The investigation on eliminating preformed fibrils, however, has rarely been reported. In this paper, near-infrared femtosecond (fs) laser is applied for the destruction of preformed Aβ fibrils in conjunction with gold nanorods (AuNRs). Our results demonstrate that the 800 nm fs-laser irradiation can locally trigger the explosion of AuNRs due to the strong localized surface plasmon resonance effect. As a result, the majority of Aβ fibrils are efficiently destroyed into small fragments by the irradiation of fs-laser with a light dose less than 75 J·cm-2. Meanwhile, significant reduction of β-sheet structures is observed by thioflavin T (ThT) fluorescence measurements. In contrast, the destruction effect by continuous wave (cw) laser irradiation is much weaker with equivalent power density and irradiation time. Furthermore, the laser-induced destruction of fibrils by Au nanoparticles (AuNPs) is also investigated, which reveals that most of the Aβ fibrils remain well under the surface explosion of spherical AuNPs. Overall, our results provide a novel design for the fast destruction of amyloid fibrils locally and biocompatibly, which may have remarkable potentials in the therapy of AD.
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