Platinum (II) diamine and triamine complexes are known toreact readily with proteins, and the sulfur atom of methionine is a keytarget.  Chelation with the amide nitrogen is possible for many platinum(II) diamine complexes with peptides.  Previously, we have found that thepresence of bulk on the amine ligands can alter the stoichiometry and/orcoordination preferences in the reactions of platinum complexes with methionineand N-acetylmethioine.  Here, we have investigated the reactions ofseveral platinum(II) complexes with two model peptides, FMRF and ACTH (1-10)(sequence = SYSMEHFRWG), both of which contain an internal methionineresidue.  The platinum complexes differ in leaving groups and amount ofamine ligand bulk.  HPLC with a cation-exchange column has been used tomonitor the rates of reaction and to determine the number of products that formfor each complex.

Reaction of platinum(II) complexes with peptides

239th National Meeting (2010)

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