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 were solved at 1.85 Å and 1.95 Å 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, L; Marzo, T; Merlino, Antonello. - In: DALTON TRANSACTIONS. - ISSN 1477-9234. - 44:22(2015), pp. 10392-10398. [10.1039/c5dt01279a]
Oxaliplatin vs. cisplatin: competition experiments on their binding to lysozyme
MARASCO, DANIELAPrimo
;MERLINO, ANTONELLOUltimo
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 were solved at 1.85 Å and 1.95 Å 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.File | Dimensione | Formato | |
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