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Diastereoselective syntheses of new analogues of the farnesyltransferase inhibitor RPR 130401.
J Org Chem
October 2004
Laboratoire des Fonctions Azotées et Oxygénées Complexes de l'IRCOF, UMR 6014 CNRS, INSA and Université de Rouen, 76821 Mont St Aignan, France.
The access to several benzo[f]perhydroisoindolic analogues of farnesyltransferase inhibitors from a single dienic precursor is reported. An initial [4 + 2] cycloaddition between diphenylisobenzofuran6 and pyrrolines 11, 14, and 15 led to either the syn or the anti isomers, depending on the mode of activation of the cycloaddition. The syn diastereomers were isolated in 90% de under 12 kbar at room temperature, while their anti counterparts were obtained with the same selectivity by warming the reaction mixture to 110 degrees C in toluene at atmospheric pressure.
View Article and Find Full Text PDFThe farnesyl transferase inhibitor RPR-130401 does not alter radiation susceptibility in human tumor cells with a K-Ras mutation in spite of large changes in ploidy and lamin B distribution.
BMC Pharmacol
December 2003
U 350 INSERM, Institut Curie-Recherche, Centre Universitaire, Orsay, France.
Background: Growth inhibition by RPR-130401, a non-peptidomimetic farnesyltransferase inhibitor, was investigated without or with combined exposure to ionizing radiation in three human tumor cell lines (HCT-116, MiAPaCa-2 and A-549) bearing a point mutation in the K-Ras gene.
Results: RPR-130401 inhibited cell growth with an IC50 of 50 nM (HCT-116), 120 nM (MiAPaCa-2) and 710 nM (A-549), with a poor incidence of apoptosis. The drug brought about G1 and S phase depletion together with arrest of cells in G2 phase and induced a significant accumulation of hyperploid cells showing active S phase DNA synthesis, with HCT-116 and A-549 cells being the most and least responsive, respectively.
RPR 130401, a nonpeptidomimetic farnesyltransferase inhibitor with in vivo activity.
Ann N Y Acad Sci
February 2000
Rhône-Poulenc Rorer S.A., Centre de recherche de Vitry-Alfortville, Vitry sur Seine, France.
Combination of the novel farnesyltransferase inhibitor RPR130401 and the geranylgeranyltransferase-1 inhibitor GGTI-298 disrupts MAP kinase activation and G(1)-S transition in Ki-Ras-overexpressing transformed adrenocortical cells.
FEBS Lett
October 1999
Unité Mixte de Recherche INRA-Université de Bourgogne, Phytopharmacie et Biochimie des Interactions Cellulaires, INRA, BV 1540, 21034, Dijon, France.
To test the Kirsten-Ras (Ki-Ras) alternative prenylation hypothesis in malignant transformation, we used a novel farnesyltransferase inhibitor competitive to farnesyl-pyrophosphate, RPR130401, and a CaaX peptidomimetic geranylgeranyltransferase-1 inhibitor GGTI-298. In Ki-Ras-overexpressing transformed adrenocortical cells, RPR130401 at 1-10 microM inhibited very efficiently the [(3)H]farnesyl but not [(3)H]geranylgeranyl transfer to Ras. However, proliferation of these cells was only slightly sensitive to RPR130401 (IC(50)=30 microM).
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