The model protein hen egg white lysozyme was challenged with Oxaliplatin and Cisplatin. ESI mass spectrometry, surface plasmon resonance and thermal shift analyses demonstrate the formation of a bis-platinum adduct, though in very small amounts. Crystals of the bis-platinum adduct were obtained using two different preparations and the X-ray structures solved at 1.85 Ǻ and 1.95 Ǻ resolution. Overall, the obtained data point out that, under the analyzed conditions, the two Pt drugs have similar affinities for the protein, but bind on its surface at two non-overlapping sites. In other words, these two drugs manifest a significantly different reactivity with this model protein and do not compete for the same protein binding sites.

Oxaliplatin vs. cisplatin: Competition experiments on their binding to lysozyme / Marasco, Daniela; Messori, Luigi; Marzo, Tiziano; Merlino, Antonello. - In: DALTON TRANSACTIONS. - ISSN 1477-9226. - ELETTRONICO. - 44:(2015), pp. 10392-10398. [10.1039/c5dt01279a]

Oxaliplatin vs. cisplatin: Competition experiments on their binding to lysozyme

MESSORI, LUIGI;MARZO, TIZIANO;MERLINO, ANTONELLO
2015

Abstract

The model protein hen egg white lysozyme was challenged with Oxaliplatin and Cisplatin. ESI mass spectrometry, surface plasmon resonance and thermal shift analyses demonstrate the formation of a bis-platinum adduct, though in very small amounts. Crystals of the bis-platinum adduct were obtained using two different preparations and the X-ray structures solved at 1.85 Ǻ and 1.95 Ǻ resolution. Overall, the obtained data point out that, under the analyzed conditions, the two Pt drugs have similar affinities for the protein, but bind on its surface at two non-overlapping sites. In other words, these two drugs manifest a significantly different reactivity with this model protein and do not compete for the same protein binding sites.
2015
44
10392
10398
Marasco, Daniela; Messori, Luigi; Marzo, Tiziano; Merlino, Antonello
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Utilizza questo identificatore per citare o creare un link a questa risorsa: https://hdl.handle.net/2158/1005517
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