6533b831fe1ef96bd1298465

RESEARCH PRODUCT

Selected cytotoxic gold compounds cause significant inhibition of 20S proteasome catalytic activities

Luigi MessoriTanja SchirmeisterM. SerratriceMaria Agostina CinelluRoberta EttariChiara GabbianiLara MassaiLaura MaioreNicola Micale

subject

DrugProteasome Endopeptidase ComplexAuranofinmedia_common.quotation_subjectAntineoplastic AgentsPharmacologyBiochemistry20s proteasomeProteasome Gold compounds Anticancer drugs Enzyme inhibitionCatalysisInorganic ChemistryInhibitory Concentration 50Structure-Activity RelationshipGold CompoundsCoordination ComplexesAuranofinmedicineHumansCytotoxic T cellmedia_commonchemistry.chemical_classificationCytotoxinsChemistryEnzymeProteasomeBiochemistryBiocatalysisOrganogold CompoundsProteasome Inhibitorsmedicine.drug

description

Abstract Six structurally diverse cytotoxic gold compounds are reported to cause profound and differential inhibition of the three main catalytic activities of purified 20S proteasome whilst auranofin , an established gold(I) drug in clinical use, is nearly ineffective. In particular, the gold(I) complex [( pbiH ) Au ( PPh 3 )] PF 6 , turns out to be the most potent inhibitor of all three enzyme activities with sub-micromolar IC 50 values. The present results further support the view that proteasome inhibition may play a major – yet not exclusive – role in the cytotoxic actions of gold based anticancer agents.

yearjournalcountryeditionlanguage
2014-01-01
10.1016/j.jinorgbio.2014.08.001http://hdl.handle.net/11568/559467