title: Interaction of Cis- and Trans-RuCl (2)(DMSO)(4) With Human Serum Albumin.
abstract: The interaction between cis- and trans- RuCl(2)(DMSO)(4) and human serum albumin have been investigated through UV-Vis, circular dichroism, fluorescence spectroscopy and inductively couplet plasma atomic emission spectroscopy (ICP(AES)) method Albumin can specifically bind 1 mole of cis-isomer and 2 moles of the trans-isomer RuCl(2)(DMSO)(4) complex. The interaction of RuCl(2)(DMSO)(4) with HSA causes: a conformational change with the loss of helical stability of protein; the strong quenching of the Trp 214 fluorescence indicating that the conformational change of the hydrophobic binding pocked in subdomain IIA takes place; a local perturbation of the warfarin binding site and induce some conformational changes at neighbour domains, a changing of the binding abilities towards heme.
authors.affiliation: Faculty of Chemistry University of Wroclaw F.Joliot Curie 14 Wroclaw 50-383 Poland.
authors.forename: L
authors.initials: L
authors.lastname: Trynda-Lemiesz
authors.forename: H
authors.initials: H
authors.lastname: Kozlowski
authors.forename: N
authors.initials: N
authors.lastname: Katsaros