1163136-86-4Relevant articles and documents
Inhibition of LDL oxidation and inflammasome assembly by nitroaliphatic derivatives. Potential use as anti-inflammatory and anti-atherogenic agents
Cataldo, Nicolás,Musetti, Bruno,Celano, Laura,Carabio, Claudio,Cassina, Adriana,Cerecetto, Hugo,González, Mercedes,Thomson, Leonor
, p. 178 - 186 (2018/10/15)
We have previously shown the antioxidant and anti-inflammatory properties of several para-substituted arylnitroalkenes. Since oxidative stress and inflammation are key processes that drive the initiation and progression of atherosclerosis, in the present work the antioxidant, anti-inflammatory and anti-atherogenic properties of an extended library of aryl-nitroaliphatic derivatives, including several newly designed nitroalkanes, was explored. The antioxidant capacity of the nitroaliphatic compounds, measured using the oxygen radical absorbance capacity assay (ORAC) showed that the p-methylthiophenyl-derivatives were about three times more effective than Trolox to prevent fluorescein oxidation, independently of the presence or the absence of the double bond next to the nitro group. The peroxyl radical scavenger capacity of the p-dimethylaminophenyl-derivatives was even higher, being the reduced form of these compounds even more active. In fact, while the antioxidant capacity of 1-dimethylamino-4-(2-nitro-1Z-ethenyl)benzene and 1-dimethylamino-4-(2-nitro-1Z-propenyl)benzene was 4.2 ± 0.1 and 5.4 ± 0.1 Trolox Eq/mol, respectively; ORAC values obtained with the ethyl and the propyl derivatives were 10 ± 1 and 13 ± 2 Trolox Eq/mol, respectively. The p-dimethylamino-derivatives, especially the nitroalkanes, were also able to prevent LDL oxidation mediated by peroxyl radicals. Oxygen consumption due to the oxidation of fatty acids was delayed in the presence of the dimethylamino substituted compounds, only the alkanes interrupted the chain of lipid oxidations decreasing the rate of oxygen consumption. Although the formation of foam cells in the presence of oxidized-LDL (oxLDL) remained unaffected, the molecules containing the dimethylamino moiety were able to decrease the expression of IL-1β in LPS/INF-γ challenged macrophages.
Structure-based insight into the asymmetric bioreduction of the C=C double bond of α,β-unsaturated nitroalkenes by pentaerythritol tetranitrate reductase
Toogood, Helen S.,Fryszkowska, Anna,Hare, Victoria,Fisher, Karl,Roujeinikova, Anna,Leys, David,Gardiner, John M.,Stephens, Gill M.,Scrutton, Nigel S.
experimental part, p. 2789 - 2803 (2009/10/20)
Biocatalytic reduction of α- or β-alkyl-barylnitroalkenes provides a convenient and efficient method to prepare chiral substituted nitroalkanes. Pentaerythritol tetranitrate reductase (PETN reductase) from Enterobacter cloacae st. PB2 catalyses the reduction of nitroolefins such as 1-nitrocyclohexene (1) with steady state and rapid reaction kinetics comparable to other old yellow enzyme homologues. Furthermore, it reduces 2-aryl-1-nitropropenes (4a-d) to their equivalent (S)-nitropropanes 9a-d. The enzyme shows a preference for the (Z)-isomer of substrates 4a-d, providing almost pure enantiomeric products 9a-d (ees up to > 99%) in quantitative yield, whereas the respective (E)-isomers are reduced with lower enantioselectivity (63-89% ee) and lower product yields. 1-Aryl-2-nitropropenes (5a, b) are also reduced efficiently, but the products (R)-10 have lower optical purities. The structure of the enzyme complex with 1-nitrocyclohexene (1) was determined by X-ray crystallography, revealing two substrate-binding modes, with only one compatible with hydride transfer. Models of nitropropenes 4 and 5 in the active site of PETN reductase predicted that the enantioselectivity of the reaction was dependent on the orientation of binding of the (E)- and (Z)- substrates. This work provides a structural basis for understanding the mechanism of asymmetric bioreduction of nitroalkenes by PETN reductase.
Lipase catalyzed kinetic resolution of α-phenyl-2-nitroalcohols
Borah, Jagat C.,Boruwa, Joshodeep,Kalita, Biswajit,Hazarika, Ajit K.,Barua, Nabin C.
, p. 1961 - 1965 (2007/10/03)
It has been demonstrated that optically pure (S)-α-phenyl-2- nitroalcohols can be efficiently prepared by kinetic resolution of the corresponding 2-nitroalcohols involving amino lipase from Pseudomonas fluorescens. In the case of β-phenyl-2-nitroalcohols, the corresponding (R)-acetates are also obtained in good optical and chemical yield along with the (S)-alcohols.
