4642-43-7Relevant articles and documents
Synthesis and evaluation of aromatic methoxime derivatives against five postharvest phytopathogenic fungi of fruits. Main structure–activity relationships
Cortés, Iván,di Liberto, Melina G.,Kaufman, Teodoro S.,Derita, Marcos G.,Bracca, Andrea B.J.
, (2020/04/15)
The antifungal activity of a library of twenty-four aromatic methoximes was examined against five representative postharvest phytopathogenic fungi. The panel included Penicillium digitatum, Penicillium italicum, Rhizopus stolonifer, Botrytis cinerea and Monilinia fructicola, all of which cause relevant economic losses worldwide as a result of affecting harvested fruits. The minimum inhibitory concentrations and minimum fungicidal concentrations of each compound were defined and the main structure–activity relationships were determined. Although other congeners were more potent, drug likeliness considerations pointed to the methoxime derived from 2,4-dihydroxypropiophenone as the compound with the most suitable profile. The morphology of the colonies of the fungal strains treated with the methoxime was examined microscopically and the compound was also tested in freshly harvested peaches and oranges, exhibiting promising control profiles in both fruits, similar to those of the commercial agents Imazalil and Carbendazim.
Computational design of a red fluorophore ligase for site-specific protein labeling in living cells
Liu, Daniel S.,Nivón, Lucas G.,Richter, Florian,Goldman, Peter J.,Deerinck, Thomas J.,Yao, Jennifer Z.,Richardson, Douglas,Phipps, William S.,Ye, Anne Z.,Ellisman, Mark H.,Drennan, Catherine L.,Baker, David,Ting, Alice Y.
, p. E4551 - E4559 (2015/02/19)
Chemical fluorophores offer tremendous size and photophysical advantages over fluorescent proteins but are much more challenging to target to specific cellular proteins. Here, we used Rosetta-based computation to design a fluorophore ligase that accepts the red dye resorufin, starting from Escherichia coli lipoic acid ligase. X-ray crystallography showed that the design closely matched the experimental structure. Resorufin ligase catalyzed the site-specific and covalent attachment of resorufin to various cellular proteins genetically fused to a 13-aa recognition peptide in multiple mammalian cell lines and in primary cultured neurons. We used resorufin ligase to perform superresolution imaging of the intermediate filament protein vimentin by stimulated emission depletion and electron microscopies. This work illustrates the power of Rosetta for major redesign of enzyme specificity and introduces a tool for minimally invasive, highly specific imaging of cellular proteins by both conventional and superresolution microscopies.
