Studies on the interactions between human serum albumin and trans-indazolium (bisindazole) tetrachlororuthenate(III)
- Author(s)
- Lilianna Trynda-Lemiesz, Aldona Karaczyn, Bernhard Keppler, Henryk Kozlowski
- Abstract
The interactions between HInd[RuInd2Cl4] and human serum albumin have been investigated through UV-Vis, circular dichroism (CD), fluorescence spectroscopy and the inductively coupled plasma-atomic emission spectroscopy (ICP(AES)) method. Binding of Ru(III)-indazole species to albumin has strong impact on protein structure and it influences considerably albumin binding of other molecules like warfarin, heme or metal ions. The metal complex-human serum albumin (HAS) interactions cause conformational changes with loss of helical stability of the protein and local perturbation in the domain IIA binding pocket. The relative fluorescence intensity of the ruthenium-bound HSA decreased, suggesting that perturbation around the Trp 214 residue took place. This was confirmed by the destabilization of the warfarin-binding site, which includes Trp 214, observed in the metal-bound HSA. Copyright (C) 2000 Elsevier Science Inc.
- Organisation(s)
- Department of Inorganic Chemistry
- External organisation(s)
- University of Wrocław, National Institutes of Health (NIH), Università Degli Studi di Siena
- Journal
- Journal of Inorganic Biochemistry
- Volume
- 78
- Pages
- 341-346
- No. of pages
- 6
- ISSN
- 0162-0134
- Publication date
- 2000
- Peer reviewed
- Yes
- Austrian Fields of Science 2012
- 1040 Chemistry
- Portal url
- https://ucrisportal.univie.ac.at/en/publications/63c021fa-0595-4111-b37e-594213ff0e88