160391-13-9

Upstream product

• 15687-27-1 ibuprofen 
• 71-36-3 butan-1-ol 
• 51146-56-6 (S)-ibuprofen 

Relevant academic research and scientific papers

Lipase-immobilized magnetic chitosan nanoparticles for kinetic resolution of (R,S)-ibuprofen

Chitosan (CS)-poly[N-benzyl-2-(methacryloxy)-N,N-dimethylethanaminium bromide] coated magnetic nanoparticles were prepared by co-precipitation method via epichlorohydrin CS cross-linking reaction and were used in the kinetic resolution of (R,S)-ibuprofen by enantioselective esterification. Enzyme immobilized onto the surface of the new magnetic supports with the use of N-(3- dimethylaminopropyl)-N′-ethylcarbodiimide hydrochloride (EDC)/N-hydroxysulfo-succinimide sodium salt (sulfo-NHS) procedure demonstrated high catalytic activity that enabled us to obtain (S)-methyl ester of ibuprofen with high enantioselectivity (E = 50.6). The chiral compounds that resulted from the application of magnetic nanoparticles were analyzed with the use of chiral stationary phases. It should be emphasized that the main advantage of the support is the possibility to magnetically recovery and effective separation (even up to 5 s) from the reaction mixture with the use of magnet. The properties of magnetic particles allow for better optimization and may reduce the total costs of the esterification reaction of ibuprofen. Moreover, the application of lipase-immobilized magnetic supports enables to maintain high enantioselective activity after repeated use.

Optimized hybrid nanospheres immobilizing Rhizomucor miehei lipase for chiral biotransformation

In this study, the immobilization of Rhizomucor miehei lipase into hybrid nanospheres containing a liposomal core was reported. Organic internal liposomal enzyme phase was protected by inorganic silica matrix, obtained with and without surfactant, that st

Synthesis, characterization and in vitro hydrolysis studies of ester and amide prodrugs of dexibuprofen

Ten prodrugs of dexibuprofen having ester and amide moieties instead of free carboxylic acid which involves in gastrointestinal side effects have been synthesized. Dexibuprofen acid chloride was condensed with different amino acid methyl ester hydrochlorides and five alcohols to afford the amide and ester prodrugs. All of the synthesized prodrugs were characterized by their mp, Rf, elemental analysis, FTIR, 1H NMR, and 13C NMR spectroscopy. The in vitro hydrolysis studies in plasma reflect prodrugs have been varied in terms of reactivity toward hydrolysis, owing to the different chemical structures. In alkyl substitution the branched chain alkyl substituents or aromatic substituents resulted in enhanced lipophilicity but diminished dissolution and hydrolysis rate. The amide prodrugs with branched and aromatic substitution can also be considered for sustained release. Prodrugs are less irritating to gastric mucosa than dexibuprofen. Springer Science+Business Media, LLC 2011.

A great improvement of the enantioselectivity of lipase-catalyzed hydrolysis and esterification using co-solvents as an additive

Addition of co-solvents such as tetrahydrofuran resulted in a great improvement of the enantioselectivity of lipase-catalyzed hydrolysis of butyl 2-(4-substituted phenoxy)propanoates in an aqueous buffer solution. On the other hand, lipase lyophilized from an aqueous solution containing the co-solvents catalyzed highly enantioselective esterification of 2-(4-substituted phenoxy)propionic acids, 2-(4-isobutylphenyl)propionic acid (ibuprofen), and 2-(6-methoxy-2-naph-thyl)propionic acid (naproxen) in an organic solvent. An increase in the E value up to two orders of magnitude was observed for some substrates. The origin of the enantioselectivity enhancement caused by the co-solvent addition was mainly attributed to a significant deceleration in the initial reaction rate for the incorrectly binding enantiomer, as compared with that for the correctly binding enantiomer. From the results of FT-1R, CD, and ESR spectra, the co-solvent addition was also found to bring about a partial destruction of the tertiary structure of lipase.