Studies of the binding of a series of platinum(IV) complexes to plasma proteins.
The platinum(IV) complexes: [PtCl(4)(en)], cis,trans-[PtCl(2)(OAc)(2)(en)], cis,trans-[PtCl(2)(OH)(2)(en)] and trans-[Pt(OH)(2)(ethmal)(en)], encompassing a range of reduction potentials and their platinum(II) analogue [PtCl(2)(en)], have been assayed for their protein binding ability in the presence of albumin, albumin and L-cysteine and RPMI 1640 tissue culture medium supplemented with foetal calf serum (RPMI/FCS). cis,trans-[PtCl(4)(en)] exhibited significant protein binding in all three experiments, in a similar fashion to the platinum(II) complex, presumably as a consequence of its rapid reduction. The remaining three platinum(IV) complexes displayed little if any protein binding, with the greatest amount of binding observed in the RPMI/FCS experiment. The extent of binding in the RPMI/FCS correlated with the reduction potentials of the complexes, with the most readily reduced species binding to the greatest extent.
Dolman
Rachael C
RC
Centre for Heavy Metals Research, School of Chemistry, The University of Sydney, Sydney, NSW 2006, Australia.
Deacon
Glen B
GB
Hambley
Trevor W
TW
D000418:Albumins / Q000378:metabolism; D001798:Blood Proteins / Q000737:chemistry / Q000378:metabolism*; D003545:Cysteine / Q000378:metabolism; D005312:Fetal Blood / Q000378:metabolism; D009944:Organoplatinum Compounds / Q000097:blood / Q000737:chemistry / Q000378:metabolism*; D011485:Protein Binding
D000418:Albumins; D001798:Blood Proteins; D009944:Organoplatinum Compounds; D003545:Cysteine