000175382 001__ 175382
000175382 005__ 20190522142437.0
000175382 0247_ $$2doi$$a10.1007/s00216-011-5523-0
000175382 022__ $$a1618-2650
000175382 02470 $$2ISI$$a000300852700018
000175382 037__ $$aARTICLE
000175382 245__ $$aFragmentation methods on the balance: unambiguous top–down mass spectrometric characterization of oxaliplatin–ubiquitin binding sites
000175382 260__ $$bSpringer-Verlag
000175382 269__ $$a2012
000175382 260__ $$c2012
000175382 336__ $$aJournal Articles
000175382 500__ $$aNational Licences
000175382 520__ $$aThe interaction between oxaliplatin and the model protein ubiquitin (Ub) was investigated in a top-down approach by means of high-resolution electrospray ionization mass spectrometry (ESI-MS) using diverse tandem mass spectrometric (MS/MS) techniques, including collision-induced dissociation (CID), higher-energy C-trap dissociation (HCD), and electron transfer dissociation (ETD). To the best of our knowledge, this is the first time that metallodrug-protein adducts were analyzed for the metal-binding site by ETD-MS/MS, which outperformed both CID and HCD in terms of number of identified metallated peptide fragments in the mass spectra and the localization of the binding sites. Only ETD allowed the simultaneous and exact determination of Met1 and His68 residues as binding partners for oxaliplatin. CID-MS/MS experiments were carried out on orbitrap and ion cyclotron resonance (ICR)-FT mass spectrometers and both instruments yielded similar results with respect to number of metallated fragments and the localization of the binding sites. A comparison of the protein secondary structure with the intensities of peptide fragments generated by collisional activation of the [Ub + Pt-(chxn)] adduct [chxn = (1R,2R)-cyclohexanediamine] revealed a correlation with cleavages in solution phase random coil areas, indicating that the N-terminal beta-hairpin and alpha-helix structures are retained in the gas phase.
000175382 6531_ $$aAnticancer metallodrugs
000175382 6531_ $$aTandem mass spectrometry
000175382 6531_ $$aElectron transfer dissociation
000175382 6531_ $$aOxaliplatin
000175382 6531_ $$aUbiquitin
000175382 6531_ $$aElectron-Capture Dissociation
000175382 6531_ $$aCollision-Induced Dissociation
000175382 6531_ $$aX-Ray-Diffraction
000175382 6531_ $$aAnticancer Metallodrugs
000175382 6531_ $$aCisplatin Binding
000175382 6531_ $$aSerum-Proteins
000175382 6531_ $$aCapillary-Electrophoresis
000175382 6531_ $$aPlatinum Interactions
000175382 6531_ $$aIdentification
000175382 6531_ $$aComplexes
000175382 700__ $$aMeier, Samuel M.
000175382 700__ $$0240220$$g174689$$aTsybin, Yury O.
000175382 700__ $$0240015$$g149418$$aDyson, Paul J.
000175382 700__ $$aKeppler, Bernhard K.
000175382 700__ $$aHartinger, Christian G.
000175382 773__ $$j402$$tAnalytical and Bioanalytical Chemistry$$k8$$q2655-2662
000175382 8564_ $$uhttps://infoscience.epfl.ch/record/175382/files/216_2011_Article_5523.pdf$$zPUBLISHER'S VERSION$$s359069
000175382 909C0 $$xU11424$$0252074$$pLSMB
000175382 909C0 $$xU9$$0252010$$pLCOM
000175382 909CO $$pSB$$particle$$ooai:infoscience.tind.io:175382
000175382 917Z8 $$x148577
000175382 937__ $$aEPFL-ARTICLE-175382
000175382 973__ $$rREVIEWED$$sPUBLISHED$$aEPFL
000175382 980__ $$aARTICLE