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The fibrillization and deposition of β-amyloid protein (Aβ) are recognized
to be the pathological hallmarks of Alzheimer’s disease (AD), which signify
the need for the effective detection and inhibition of Aβ accumulation.
Development of multifunctional agents that can inhibit Aβ aggregation,
rapidly disaggregate fibrils, and image aggregates is one of the effective
strategies to treat and diagnose AD. Herein, the multifunctionality of
nitrogen-doped carbonized polymer dots (CPDs) targeting Aβ aggregation
is reported. CPDs inhibit the fibrillization of Aβ monomers and rapidly
disintegrate Aβ fibrils by electrostatic interactions, hydrogen-bonding
and hydrophobic interactions with Aβ in a time scale of seconds to
minutes. Moreover, the interactions make CPDs label Aβ fibrils and
emit enhanced red fluorescence by the binding, so CPDs can be used
for in vivo imaging of the amyloids in transgenic Caenorhabditis
elegans CL2006 as an AD model. Importantly, CPDs are demonstrated
to scavenge the in vivo amyloid plaques and to promote the lifespan
extension of CL2006 strain by alleviating the Aβ-triggered toxicity. Taken
together, the multifunctional CPDs show an exciting prospect for further
investigations in Aβ-targeted AD treatment and diagnosis, and this study
provides new insight into the development of carbon materials in AD
theranostics.