| 18475961 |
Trynda-Lemiesz L, Kozlowski H, Katsaros N: Interaction of Cis- and Trans-RuCl (2)(DMSO)(4) With Human Serum Albumin. . Met Based Drugs. 2000;7(6):293-9.
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. |
1(0,0,0,1) |