915799-68-7Relevant academic research and scientific papers
Minimal Self-Immolative Probe for Multimodal Fluoride Detection
Gabrielli, Luca,Mancin, Fabrizio
, p. 10715 - 10720 (2016/11/29)
Two single-molecule, self-immolative fluoride probes, namely tert-butyldimethylsilyl-protected 2- and 4-difluoromethylphenol, are described. Compared to similar systems previously described, the probes are characterized by a simpler structure and straightforward, two-step preparation. Nevertheless, they allow the detection of fluoride ions at micromolar concentration by the naked eye, UV-vis absorption, and fluorescence. A detailed investigation of the self-immolative reaction reveals that the rate-limiting step is the release of the first fluoride ion from the difluoromethylphenolate intermediate. Moreover, the mutual position of the difluoromethyl- and tert-butyldimethylsilyl-protected residues has a relevant effect on the reactivity. Likely, a CF2H-O hydrogen bond in the 2-isomer increases the reactivity of the silyl ether toward hydrolytic cleavage but also stabilizes the phenolate intermediate, slowing the release of fluoride ions.
Synthesis and evaluation of general mechanism-based inhibitors of sulfatases based on (difluoro)methyl phenyl sulfate and cyclic phenyl sulfamate motifs
Hanson, Sarah R.,Whalen, Lisa J.,Wong, Chi-Huey
, p. 8386 - 8395 (2008/02/05)
Several model mechanism-based inhibitors (MbIs) were designed and evaluated for their ability to inhibit sulfatases. The MbI motifs were based on simple aromatic sulfates, which are known to be commonly accepted substrates across this highly conserved enzyme class, so that they might be generally useful for sulfatase labeling studies. (Difluoro)methyl phenol sulfate analogs, constructed to release a reactive quinone methide trap, were not capable of irreversibly inactivating the sulfatase active site. On the other hand, the cyclic sulfamates (CySAs) demonstrated inhibition profiles consistent with an active site-directed mode of action. These molecules represent a novel scaffold for labeling sulfatases and for probing their catalytic mechanism.
