A dual-mode aggregative host:guest indicator displacement sensing system has been created for the detection of trimethylated peptides and determination of histone demethylase activity. The combination of selective recognition of suitably sized trimethylammonium salts and reversible lipophilic aggregation of the host:guest complex provides a unique quenching mechanism that is not only dependent on affinity for sensitivity but the lipophilicity of the indicator. In addition, aggregation can be controlled by the application of chaotropic anions in the mixture, allowing a second level of discrimination between hard lysine groups and softer trimethyllysines.

A new concept for organic light-emitting diodes (OLEDs) is presented, which is called exciplex-sensitized triplet-triplet annihilation (ESTTA). The exciplex formed at the organic heterojunction interface of 4,4',4″-tris(N-3-methyphenyl-N-phenyl-amino) triphenylamine and 9,10-bis(2'-naphthyl) anthracene (ADN) is used to sensitize the triplet-triplet annihilation (TTA) process on the ADN molecules. This results in a turn-on voltage (2.2 V) of the blue emission from the OLED below the bandgap (2.9 eV). From the transient electroluminescence measurement, blue emission totally came from the TTA process without direct recombination on the ADN molecules. The blue singlet exciton from the TTA process can be quenched by energy transfer to the exciplex, as revealed by transient photoluminescence measurements. This can be prevented by blocking the energy transfer path and improving the radiative recombination rate of blue emission. With the insertion of the "triplet diffusion and singlet blocking (TDSB)" layer and the incorporation of the dopant material, an ESTTA-OLED with external quantum efficiency of 5.1% was achieved, which consists of yellow and blue emission coming from the exciplex and ESTTA process, respectively.

Arrayed, self-folding deep cavitands form a fluorescence displacement assay system for the site-selective sensing of post-translationally modified (PTM) histone peptides.