13254-04-1Relevant articles and documents
Synthesis and antimalarial bioassay of quinine - peptide conjugates
Panda, Siva S.,Ibrahim, Mohamed A.,Kuecuekbay, Hasan,Meyers, Marvin J.,Sverdrup, Francis M.,El-Feky, Said A.,Katritzky, Alan R.
, p. 361 - 366 (2013/10/08)
Amino acid and peptide conjugates of quinine were synthesized using microwave irradiation in 52-95% yields using benzotriazole methodology. The majority of these conjugates retain in vitro antimalarial activity with IC50 values below 100 nm, similar to quinine.
Synthesis and activity of analogues of the isoleucyl tRNA synthetase inhibitor SB-203207
Crasto, Curtis F.,Forrest, Andrew K.,Karoli, Tomislav,March, Darren R.,Mensah, Lucy,O'Hanlon, Peter J.,Nairn, Michael R.,Oldham, Mark D.,Yue, Weimin,Banwell, Martin G.,Easton, Christopher J.
, p. 2687 - 2694 (2007/10/03)
Twenty two analogues of SB-203207 have been prepared by total synthesis, and evaluated as inhibitors of a range of tRNA synthetases. Changes to the bicyclic core, removing either the terminal amino substituent or the sulfonyl group from the side chain, and altering either the carbon skeleton or stereochemistry of the isoleucine residue, decreases the potency of inhibition of isoleucyl tRNA synthetase. Substituting the isoleucine residue with other amino acids produces inhibitors of the corresponding synthetases. In particular, a methionine derivative is 50-100 times more potent against methionyl tRNA synthetase than against any of the corresponding isoleucyl, leucyl, valyl, alanyl and prolyl synthetases.
