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Studies on the interactions between human serum albumin and imidazolium [trans-tetrachlorobis(imidazol)ruthenate(III)].
Autorzy
Rok wydania
1999
Czasopismo
Journal of Inorganic Biochemistry
Numer woluminu
73
Strony
123-128
DOI
10.1016/s0162-0134(99)00004-5
Kolekcja
Język
Angielski
Typ publikacji
Artykuł
The interactions between imidazolium [trans-tetrachlorobis(imidazol) ruthenate(III)] (Ru-im) and human serum albumin (HSA) have been investigated through UV-Vis, CD, fluorescence spectroscopy and by the antibody precipitation test. Binding of Ru(III)-imidazole species to albumin has a strong impact on the protein structure and influences considerably the albumin binding of other molecules such as warfarin or heme. The metal complex-HSA interactions cause conformational changes with the 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 destabilisation of the warfarin binding site which includes Trp 214, observed in the metal-bound HSA.
Adres publiczny
http://doi.org/10.1016/s0162-0134(99)00004-5
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