TY - JOUR
T1 - Studies on the interactions between human serum albumin and trans-indazolium (bisindazole) tetrachlororuthenate(III)
AU - Trynda-Lemiesz, Lilianna
AU - Karaczyn, Aldona
AU - Keppler, Bernhard
AU - Kozlowski, Henryk
N1 - Zeitschrift: Journal of Inorganic Biochemistry
DOI: 10.1016/S0162-0134(00)00062-3
Coden: JIBID
Affiliations: Faculty of Chemistry, Univ. Wroclaw, F. Joliot-C., Wroclaw, Poland; Institute of Inorganic Chemistry, Univ. Vienna, W., Vienna, Austria
Adressen: Trynda-Lemiesz, L.; Faculty of Chemistry; University of Wroclaw; F. Joliot-Curie 14 50383 Wroclaw, Poland; email: [email protected]
Source-File: ChemieErgScopus.csv
Import aus Scopus: 2-s2.0-0034737805
Importdatum: 09.01.2007 14:15:29
12.02.2008: Datenanforderung 2112 (Import Sachbearbeiter)
09.02.2010: Datenanforderung UNIVIS-DATEN-DAT.RA-2 (Import Sachbearbeiter)
PY - 2000
Y1 - 2000
N2 - 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.
AB - 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.
M3 - Article
SN - 0162-0134
VL - 78
SP - 341
EP - 346
JO - Journal of Inorganic Biochemistry
JF - Journal of Inorganic Biochemistry
IS - 4
ER -