000118310 001__ 118310
000118310 005__ 20190527123504.0
000118310 0247_ $$2doi$$a10.1021/ic702236m
000118310 02470 $$2ISI$$a000252019500006
000118310 037__ $$aARTICLE
000118310 245__ $$aCharacterization of Platinum Anticancer Drug Protein-Binding Sites Using a Top-Down Mass Spectrometric Approach
000118310 269__ $$a2008
000118310 260__ $$c2008
000118310 336__ $$aJournal Articles
000118310 520__ $$aA proof-of-principle study on the application of a top-down electrospray ionization Fourier transform ion cyclotron resonance mass spectrometric approach for characterization of the primary binding sites of the platinum anticancer agents cisplatin, transplatin, and oxaliplatin on ubiquitin is presented. Through employment of different fragmentation techniques, the binding sites of cisplatin and oxaliplatin were found at N-terminal methionine-contg. ubiquitin fragments, while transplatin was obsd. to be attached to 19Pro-Ser-Asp-Thr-Ile-Glu24. The binding to proteins is of particular relevance for the mode of action of metallodrugs with regard to (de)activation, transport, excretion, etc. To the best of our knowledge, this is the first top-down mass spectrometric study on the protein binding site characterization of transition-metal anticancer agents and demonstrates the potential of the applied technique for investigating metal drug-protein interactions.
000118310 700__ $$aHartinger, Christian G.
000118310 700__ $$0240220$$g174689$$aTsybin, Yury O.
000118310 700__ $$aFuchser, Jens
000118310 700__ $$aDyson, Paul J.$$g149418$$0240015
000118310 773__ $$j47$$tInorganic Chemistry$$k1$$q17-19
000118310 909C0 $$xU11424$$0252074$$pLSMB
000118310 909C0 $$xU9$$0252010$$pLCOM
000118310 909CO $$pSB$$particle$$ooai:infoscience.tind.io:118310
000118310 937__ $$aLCOM-ARTICLE-2008-044
000118310 937__ $$aLSMB-ARTICLE-2008-001
000118310 973__ $$rREVIEWED$$sPUBLISHED$$aEPFL
000118310 980__ $$aARTICLE