Elucidating the structure of protein aggregates is vital
for overcoming
human diseases arising from protein misfolding. It is rarely reported
that the conventional protein-amyloid fibrillation probe ThT can be
used as a STED agent to visualize protein aggregation structures at
the nanometer level, suffering from small Stokes’ shift and
photobleaching. Herein, we report a donor–acceptor (D–A)-type
fluorophore, IAD2, with red emission and a large Stokes' shift
(196
nm). It is demonstrated that IAD2 exhibited a 7.8-fold enhancement
on the fluorescence intensity and an obvious 94 nm blue shift on the
emission wavelength after binding with bovine insulin fibril, due
to the alternation of the microenvironment. Besides, IAD2 has a relatively
higher binding affinity to insulin fibrils in comparison to ThT. Molecular
docking assay also verified the binding sites and interaction forces
between IAD2 and insulin fibrils. Owing to its high depletion efficiency
and good photostability, IAD2 was utilized to stain insulin fibrils
to achieve STED imaging with a resolution of 101.2 nm. This study
will shed light on the design of novel solvatochromic fluorescent
probe for the super-resolution imaging of protein aggregate structure.