1071-71-2Relevant articles and documents
New TRAP1 and Hsp90 chaperone inhibitors with cationic components: Preliminary studies on mitochondrial targeting
Rondanin,Lettini,Oliva,Baruchello,Costantini,Trapella,Simoni,Bernardi,Sisinni,Pietrafesa,Ponterini,Costi,Vignudelli,Luciani,Matassa,Esposito,Landriscina
, p. 2289 - 2293 (2018)
TRAP1 (Hsp75) is the mitochondrial paralog of the Hsp90 molecular chaperone family. Due to structural similarity among Hsp90 chaperones, a potential strategy to induce apoptosis through mitochondrial TRAP1 ATPase inhibition has been envisaged and a series of compounds has been developed by binding the simple pharmacophoric core of known Hsp90 inhibitors with various appendages bearing a permanent cationic head, or a basic group highly ionizable at physiologic pH. Cationic appendages were selected as vehicles to deliver drugs to mitochondria. Indeed, masses of new derivatives were evidenced to accumulate in the mitochondrial fraction from colon carcinoma cells and a compound in the series, with a guanidine appendage, demonstrated good activity in inhibiting recombinant TRAP1 ATPase and cell growth and in inducing apoptotic cell death in colon carcinoma cells.
Avidin and streptavidin ligands based on the glycoluril bicyclic system
Hidalgo-Fernandez, Pedro,Ayet, Eva,Canal, Ivan,Farrera, Joan-Antoni
, p. 3147 - 3154 (2006)
Glycoluril derivatives with a carboxylic acid side chain have been synthesized and shown to bind to both avidin and streptavidin. Introduction of a valerate side chain in glycoluril led to an increased binding to both proteins only when the valerate group was bound to a N atom and with the proper stereochemistry [(+)-enantiomer]. On the other hand, introduction of the valerate side chain either on the bridgehead carbon or on the N atom with the opposite stereochemistry [(-)-enantiomer] led to a decrease in binding constant compared with unsubstituted glycoluril. Direct spectrophotometric competitive titration of each protein with a racemic ligand allowed measurement of the enantioselectivity of the ligand-protein complexation, together with the binding constant of the two enantiomers. In the case of the N-substituted glycoluril, the extension of the side chain by one methylene group, from valerate to caproate, led to an increase in the binding constant to both proteins. Docking studies using AutoDock 3.05 have been performed in order to predict the binding modes of these ligands to streptavidin. The effect of the stereochemistry and the position of the side chain on the binding constant to streptavidin is discussed in view of the predicted binding modes. The Royal Society of Chemistry 2006.
Palladium-catalyzed allylic alkylation of carboxylic acid derivatives: N-acyloxazolinones as ester enolate equivalents
Trost, Barry M.,Michaelis, David J.,Charpentier, Julie,Xu, Jiayi
supporting information; experimental part, p. 204 - 208 (2012/02/16)
Triple A: A general asymmetric allylic alkylation of ester enolate equivalents at the carboxylic acid oxidation state is reported. N-Acylbenzoxazolinone-derived enol carbonates were synthesized and employed in the palladium-catalyzed alkylation reaction. The imide products were readily converted into a series of carboxylic acid derivatives without loss of enantiopurity.
