International audienceA probe to detect specific peptidases based on the unique solid-state fluorophore HPQ has been developed by the use of an autoimmolative cyclization spacer in conjunction with an acylated O,O-acetal linked to HPQ (see scheme). Under our assay conditions this probe detected the enzyme with a minimum half-time of only 560 s

No abstract

No abstract

A series of structurally simple bibenzyl-diol and stilbene-diol core molecules, structural analogs of the well-known hexestrol and diethylstilbestrol non-steroidal estrogens, were prepared and evaluated as estrogen receptor (ER) subtype-selective ligands. Analysis of their ERα and ERβ binding showed that certain substitution patterns engendered binding affinities that were >100-fold selective for ERβ. When further investigated in cell-based gene transcription assays, some molecules showed similarly high relative transcriptional potency selectivity in favor of ERβ. Interestingly, the most ERβ-selective molecules were those bearing non-polar substituents on one of the internal carbon atoms. These compounds should be useful probes for determining the physiological roles of ERβ, and they might lead to the development of more selective and thus safer pharmaceuticals.