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

Dalton Trans. 2015 Jun 14;44(22):10392-8. doi: 10.1039/c5dt01279a.

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.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Antineoplastic Agents / metabolism*
  • Binding Sites
  • Circular Dichroism
  • Cisplatin / metabolism*
  • Crystallography
  • Muramidase / metabolism*
  • Organoplatinum Compounds / metabolism*
  • Oxaliplatin
  • Protein Binding
  • Spectrometry, Mass, Electrospray Ionization
  • Surface Plasmon Resonance

Substances

  • Antineoplastic Agents
  • Organoplatinum Compounds
  • Oxaliplatin
  • hen egg lysozyme
  • Muramidase
  • Cisplatin