Electrospray ionization high resolution mass spectrometry was used to explore the interactions occurring between metal complexes and proteins/peptides. In a first study three medicinally relevant compounds, cisplatin, transplatin and the organometallic ruthenium compound RAPTA-C, were reacted with a pool of three proteins, ubiquitin, cytochrome c and superoxide dismutase, and the reaction products were analysed using high resolution mass spectrometry. The formation of metal-protein adducts was clearly observed for the three proteins. In addition, valuable information was obtained on the nature of the protein-bound metallofragments, on their distribution among the three different proteins and on the binding kinetics. The platinum compounds were less reactive and considerably less selective in protein binding than RAPTA-C, which showed a high affinity towards ubiquitin and cytochrome c, but not superoxide dismutase. In addition, competition studies between cisplatin and RAPTA-C showed that the two metallodrugs upon protein binding manifest high affinity for the same amino acid residues. In a second study the ruthenium complex fac-[Ru(CO)3Cl2(N1-thz)] was reacted with two peptides, human β amyloid 1-42 and human β amyloid 1-28, and the reaction products were analysed using high resolution mass spectrometry. The MS spectra suggested a prevalent 1:1 metal-peptides stoichiometry and disclosed the nature of peptide-bound metallic fragments.

Exploring metal complexes-protein/peptide interactions by high resolution mass spectrometry / Elena Michelucci, Chiara Gabbiani, Angela Casini, Giuseppe Pieraccini, Gloriano Moneti, Daniela Valensin, Luigi Messori. - STAMPA. - (2009), pp. 12-12. (Intervento presentato al convegno Alta risoluzione, imaging, ion mobility: le sfide della spettrometria di massa moderna).

Exploring metal complexes-protein/peptide interactions by high resolution mass spectrometry

Elena Michelucci;Chiara Gabbiani;Angela Casini;Giuseppe Pieraccini;Gloriano Moneti;Luigi Messori
2009

Abstract

Electrospray ionization high resolution mass spectrometry was used to explore the interactions occurring between metal complexes and proteins/peptides. In a first study three medicinally relevant compounds, cisplatin, transplatin and the organometallic ruthenium compound RAPTA-C, were reacted with a pool of three proteins, ubiquitin, cytochrome c and superoxide dismutase, and the reaction products were analysed using high resolution mass spectrometry. The formation of metal-protein adducts was clearly observed for the three proteins. In addition, valuable information was obtained on the nature of the protein-bound metallofragments, on their distribution among the three different proteins and on the binding kinetics. The platinum compounds were less reactive and considerably less selective in protein binding than RAPTA-C, which showed a high affinity towards ubiquitin and cytochrome c, but not superoxide dismutase. In addition, competition studies between cisplatin and RAPTA-C showed that the two metallodrugs upon protein binding manifest high affinity for the same amino acid residues. In a second study the ruthenium complex fac-[Ru(CO)3Cl2(N1-thz)] was reacted with two peptides, human β amyloid 1-42 and human β amyloid 1-28, and the reaction products were analysed using high resolution mass spectrometry. The MS spectra suggested a prevalent 1:1 metal-peptides stoichiometry and disclosed the nature of peptide-bound metallic fragments.
2009
Alta risoluzione, imaging, ion mobility: le sfide della spettrometria di massa moderna, Milano, 16 dicembre 2009
Alta risoluzione, imaging, ion mobility: le sfide della spettrometria di massa moderna
Elena Michelucci, Chiara Gabbiani, Angela Casini, Giuseppe Pieraccini, Gloriano Moneti, Daniela Valensin, Luigi Messori
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Utilizza questo identificatore per citare o creare un link a questa risorsa: https://hdl.handle.net/2158/1117366
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