856906-98-4Relevant academic research and scientific papers
Novel inhibitors of Staphylococcus aureus RnpA that synergize with mupirocin
Lounsbury, Nicole,Eidem, Tess,Colquhoun, Jennifer,Mateo, George,Abou-Gharbia, Magid,Dunman, Paul M.,Childers, Wayne E.
supporting information, p. 1127 - 1131 (2018/02/21)
We recently discovered RnpA as a promising new drug discovery target for methicillin-resistant S. aureus (MRSA). RnpA is an essential protein that is thought to perform two required cellular processes. As part of the RNA degrasome Rnpa mediates RNA degradation. In combination with rnpB it forms RNase P haloenzymes which are required for tRNA maturation. A high throughput screen identified RNPA2000 as an inhibitor of both RnpA-associated activities that displayed antibacterial activity against clinically relevant strains of S. aureus, including MRSA. Structure-activity studies aimed at improving potency and replacing the potentially metabotoxic furan moiety led to the identification of a number of more potent analogs. Many of these new analogs possessed overt cellular toxicity that precluded their use as antibiotics but two derivatives, including compound 5o, displayed an impressive synergy with mupirocin, an antibiotic used for decolonizing MSRA whose effectiveness has recently been jeopardized by bacterial resistance. Based on our results, compounds like 5o may ultimately find use in resensitizing mupirocin-resistant bacteria to mupirocin.
Furan derivatives of substituted phenylthiourea: Spectral studies, semi-empirical quantum-chemical calculations and X-ray structure analyses
Hritzova?, Ol'ga,?ernák, Juraj,?afa?, Peter,Frohlichová, Zdenka,Csoregh, Ingeborg
, p. 29 - 48 (2007/10/03)
Fifty new derivatives of 1-(furan-2-carbonyl)- and 1-(furan-3-carbonyl)-3- phenyl substituted thiourea have been synthesised and identified. Intramolecular hydrogen bonds were investigated in detail, using IR spectroscopy. The three-level Fermi resonance
