Interaction of serum albumins with cluster rhenium compounds of cis- and trans-configuration

Abstract

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

Daunomycin-loaded superparamagnetic iron oxide nanoparticles: Preparation, magnetic targeting, cell cytotoxicity, and protein delivery research

“…As is shown in Figure 9, the fluorescence intensity decreased regularly with the titration of SPION-DNM, indicating that the drug delivery alters the spatial structure of HSA and therefore increases the exposure of Trp-212 to the medium indirectly, which leads to a less hydrophobic environment of the fluorescence chromophore placed. 28,29 The newly appeared shoulder peak located at 310 nm could be attributed to the new state of SPION-DNM bound HSA, 30 which also confirms the tight binding between the nanospheres and protein.…”

“…As has been thoroughly emphasized, the fluorescence of Trp and Tyr residues is highly sensitive to the polarity of its environment, which usually presents a red shift in a more polar surrounding. [27][28][29][30] Thus, the emission shifts of the amino acid residues could be employed to examine the conformational changes of protein. To further probe the binding mechanism of the SPION-DNM nanospheres and HSA, synchronous fluorescence spectroscopy experiment was carried out to investigate the conformational changes of protein.…”

Rhenium–platinum antitumor systems

“…We investigated differences in the interactions between binuclear cluster rhenium(III) compounds of cis-and trans-configuration with native bovine serum albumin (BSA) and human serum albumin (HSA) by methods of electronic absorbtion spectroscopy, tryptophan fluorescence and circular dichroism spectroscopy [94]. It was shown that in the process of interaction of both compounds with proteins the formation of the different complexes took place via His moieties with preservation of quadruple Re-Re bond.…”

Changes in oxidative stress intensity in blood of tumor-bearing rats following different modes of administration of rhenium-platinum system

“…Fluorescence was measured in phosphate buffer pH 7.4 using spectrofluorimeter Shimadzu RF-5301 PC (Japan), slit width EX: 10.0 nm and EM: 10.0 nm, excitation wavelength 290 nm [8]. The effect of the compound i in a molar ratio of 1(SOD):10(i) was studied immediately after mixing.…”