114223-14-2Relevant academic research and scientific papers
Design and structural analysis of aromatic inhibitors of type II dehydroquinase from mycobacterium tuberculosis
Howard, Nigel I.,Dias, Marcio V.B.,Peyrot, Fabienne,Chen, Liuhong,Schmidt, Marco F.,Blundell, Tom L.,Abell, Chris
, p. 116 - 133 (2015/04/14)
3-Dehydroquinase, the third enzyme in the shikimate pathway, is a potential target for drugs against tuberculosis. Whilst a number of potent inhibitors of the Mycobacterium tuberculosis enzyme based on a 3-dehydroquinate core have been identified, they generally show little or no in vivo activity, and were synthetically complex to prepare. This report describes studies to develop tractable and drug-like aromatic analogues of the most potent inhibitors. A range of carbon-carbon linked biaryl analogues were prepared to investigate the effect of hydrogen bond acceptor and donor patterns on inhibition. These exhibited inhibitory activity in the high-micromolar range. The addition of flexible linkers in the compounds led to the identification of more potent 3-nitrobenzylgallate- and 5-aminoiso-phthalate-based analogues.
Novel chemoselective de-esterification of esters of polyacetoxy aromatic acids by lipases
Parmar, Virinder S.,Kumar, Ajay,Bicht, Kirpal S.,Mukherjee, Shubhasish,Prasad, Ashok K.,Sharma, Sunil K.,Wengel, Jesper,Olsen, Carl E.
, p. 2163 - 2176 (2007/10/03)
Candida cylindracea lipase (CCL) and porcine pancreatic lipase (PPL) have been used for deacetylation of peracetates of methyl and ethyl esters of six different polyphenolic acids in organic solvents. Exclusive de-esterification of the ester groups derived from the phenolic hydroxy and aliphatic acid over the ester group of the aromatic acid and aliphatic alcohol has been achieved affording the corresponding esters of phenolic acids in as high yields as 90-97%. The results have been corroborated with the mechanism of lipase action.
