Journal article

A mass spectrometric and molecular modelling study of cisplatin binding to transferrin

A combination of mass spectrometry, UV/Vis spectroscopy and molecular modelling techniques hove been used to characterise the interaction of cisplatin with human serum transferrin (Tf). Mass spectrometry indicates that cisplatin binds to the hydroxy functional group of threonine 457, which is located in the iron(III)-binding site on the C-terminal lobe of the protein. UV/Vis spectroscopy confirms the stoichiometry of binding and shows that cisplatin and iron(m) binding are competitive. The binding of cisplatin has been modelled by using molecular dynamic simulotions and the results suggest that cisplatin can occupy part of both the iron(III)- and carbonate-binding sites in the C-terminal lobe of the protein. Combined, the studies suggest that cisplatin binding sterically restricts iron(m) binding to the C-terminal lobe binding site, whereas the N-terminal lobe binding site appears to be unaffected by the cisplatin interaction, possibly allowing the iron (III)-induced conformational change necessary for binding to a Tf receptor.


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