1183501-24-7Relevant academic research and scientific papers
A Reduced-Symmetry Heterobimetallic [PdPtL4]4+ Cage: Assembly, Guest Binding, and Stimulus-Induced Switching
Crowley, James D.,Findlay, James A.,Hartinger, Christian G.,Lisboa, Lynn S.,Wright, L. James
, p. 11101 - 11107 (2020)
A strategy is presented that enables the quantitative assembly of a heterobimetallic [PdPtL4]4+ cage. The presence of two different metal ions (PdII and PtII) with differing labilities enables the cage to be opened and closed selectively at one end upon treatment with suitable stimuli. Combining an inert PtII tetrapyridylaldehyde complex with a suitably substituted pyridylamine and PdII ions led to the assembly of the cage. 1H and DOSY NMR spectroscopy and ESI mass spectrometry data were consistent with the quantitative formation of the cage, and the heterobimetallic structure was confirmed using single-crystal X-ray crystallography. The structure of the host–guest adduct with a 2,6-diaminoanthraquinone guest molecule was determined. Addition of N,N′-dimethylaminopyridine (DMAP) resulted in the formation of the open-cage [PtL4]2+ compound and [Pd(DMAP)4]2+ complex. This process could then be reversed, with the reformation of the cage, upon addition of p-toluenesulfonic acid (TsOH).
Structure-activity relationships of substituted 1-pyridyl-2-phenyl-1,2- ethanediones: Potent, selective carboxylesterase inhibitors
Young, Brandon M.,Hyatt, Janice L.,Bouck, David C.,Chen, Taosheng,Hanumesh, Parimala,Price, Jeanine,Boyd, Vincent A.,Potter, Philip M.,Webb, Thomas R.
supporting information; experimental part, p. 8709 - 8715 (2011/02/23)
Inhibition of intestinal carboxylesterases may allow modification of the pharmacokinetics/pharmacodynamic profile of existing drugs by altering half-life or toxicity. Since previously identified diarylethane-1,2-dione inhibitors are decidedly hydrophobic,
