Elucidation of the binding sites of two novel Ru(II) complexes on bovine serum albumin.

Elucidation of the binding sites of two novel Ru(II) complexes on bovine serum albumin.
J Inorg Biochem. 2016 Mar 2;159:89-95
Authors: Nišavić M, Masnikosa R, Butorac A, Perica K, Rilak A, Korićanac L, Hozić A, Petković M, Cindrić M
Abstract
Hyphenated mass spectrometry (MS) techniques have attained an important position in analysis of covalent and non-covalent interactions of metal complexes with peptides and proteins. The aim of the present study was to qualitatively and quantitatively determine ruthenium binding sites on a protein using tandem mass spectrometry and allied techniques, i.e. liquid chromatography (LC) and inductively coupled plasma optical emission spectrometry (ICP-OES). For that purpose, two newly synthesized Ru(II) complexes of a meridional geometry, namely mer-[Ru(4' Cl-tpy)(en)Cl](+) (1) and mer-[Ru(4' Cl-tpy)(dach)Cl](+) (2) (where 4' Cl-tpy=4'-chloro-2,2':6',2″-terpyridine, en=1,2-diaminoethane and dach=1,2-diaminocyclohexane), and bovine serum albumin were used. The binding of the complexes to the protein was investigated by means of size exclusion- and reversed phase-LC, ICP OES, matrix-assisted laser desorption ionization MS and MS/MS. Ruthenated peptide sequence and a binding target amino acid were revealed through accurate elucidation of MS/MS spectra. The results obtained in this study suggest a high binding capacity of the protein towards both complexes, with up to 5.77±0.14 and 6.95±0.43mol o...

Source: Journal of Inorganic Biochemistry - March 2, 2016 Category: Biochemistry Authors: Nišavić M, Masnikosa R, Butorac A, Perica K, Rilak A, Korićanac L, Hozić A, Petković M, Cindrić M Tags: J Inorg Biochem Source Type: research