Leus I.V.,Dnipropetrovsk National University |
Klenina I.O.,Institute of Gastroenterology AMSU |
Zablotska K.A.,Ukrainian State University of Chemical Technology |
Golichenko O.A.,Ukrainian State University of Chemical Technology |
And 2 more authors.
Biopolymers and Cell | Year: 2011
Aim. To investigate differences in the interactions of binuclear cluster rhenium(III) compounds of cis(I)- and trans(II)-configuration with bovine serum albumin (BSA) and human serum albumin (HSA). Methods. Electronic spectroscopy, tryptophan fluorescence and circular dichroism spectroscopy. Results. It was shown that in the process of interaction of I and II with proteins different complexes were formed where the quadruple bond Re-Re remained. Conclusions. It is proposed that the trans-isomer interacts with molecular environment of Trp-214 (HSA) and Trp-212 (BSA) in hydrophobic pocket of the IIA subdomain of homological proteins. For the cis-isomer more complex mechanism operates that includes not only the subdomain IIA, but also at least one more binding site for the rhenium compound in the subdomain IB of the proteins. Different influence of I and II on the secondary structure of homological proteins has been shown. © Institute of Molecular Biology and Genetics, NAS of Ukraine, 2011. Source