54981-87-2Relevant articles and documents
Nickel-Catalyzed C(sp3)-C(sp3) Cross-Electrophile Coupling of in Situ Generated NHP Esters with Unactivated Alkyl Bromides
Kang, Kai,Weix, Daniel J.
supporting information, p. 2853 - 2857 (2022/05/03)
The formation of C(sp3)-C(sp3) bonds by cross-coupling remains a challenge in synthesis. Here, we demonstrate a two-step, one-pot protocol for the in situ generation of N-hydroxyphthalimide esters and their nickel-catalyzed cross-electrophile coupling with unactivated alkyl bromides for the construction of 1°/1 ° C(sp3)-C(sp3) bonds. The conditions tolerate an array of functional groups, and mechanistic studies indicate that both substrates are converted to alkyl radicals during the reaction.
Asymmetric Photocatalytic C-H Functionalization of Toluene and Derivatives
Mazzarella, Daniele,Crisenza, Giacomo E. M.,Melchiorre, Paolo
supporting information, p. 8439 - 8443 (2018/07/25)
Reported herein is a visible-light-mediated organocatalytic direct C-H functionalization of toluene derivatives to afford enantioenriched β-benzylated aldehydes from the corresponding enals. The process combines the oxidative power of a chiral excited-state iminium ion and the basic nature of its counteranion to trigger the generation of benzylic radicals by means of a sequential multisite proton-coupled electron transfer mechanism. This study shows that feedstock chemicals generally used as solvents, such as toluene and xylene derivatives, can be used as substrates for making chiral molecules with high enantioselectivity.
X-ray crystal structures of Enterococcus faecalis thymidylate synthase with folate binding site inhibitors
Catalano, Alessia,Luciani, Rosaria,Carocci, Alessia,Cortesi, Debora,Pozzi, Cecilia,Borsari, Chiara,Ferrari, Stefania,Mangani, Stefano
, p. 649 - 664 (2016/08/12)
Infections caused by Enterococcus faecalis (Ef) represent nowadays a relevant health problem. We selected Thymidylate synthase (TS) from this organism as a potential specific target for antibacterial therapy. We have previously demonstrated that species-specific inhibition of the protein can be achieved despite the relatively high structural similarity among bacterial TSs and human TS. We had previously obtained the EfTS crystal structure of the protein in complex with the metabolite 5-formyl-tetrahydrofolate (5-FTHF) suggesting the protein role as metabolite reservoir; however, protein–inhibitors complexes were still missing. In the present work we identified some inhibitors bearing the phthalimidic core from our in-house library and we performed crystallographic screening towards EfTS. We obtained two X-ray crystallographic structures: the first with a weak phthalimidic inhibitor bound in one subunit and 5-hydroxymethylene-6-hydrofolic acid (5-HMHF) in the other subunit; a second X-ray structure complex with methotrexate. The structural information achieved confirm the role of EfTS as an enzyme involved in the folate pool system and provide a structural basis for structure-based drug design.
