Biopolym. Cell. 2011; 27(6):465-471.
http://dx.doi.org/10.7124/bc.000119
Structure and Function of Biopolymers
Interaction of serum albumins with cluster rhenium compounds of cis- and trans-configuration
1Leus I. V., 2Klenina I. O., 3Zablotska K. A., 3Golichenko O. A., 3Shtemenko O. V., 1Shtemenko N. I.
  1. Oles Honchar Dnipropetrovsk National University
    72, Gagarin Av., Dnipropetrovs'k, Ukraine, 49050
  2. Institute of Gastroenterology AMSU
    96, Newspaper "Pravda" av., Dnipropetrovs'k, Ukraine, 49074
  3. Ukrainian State University of Chemical Technology
    8, Gagarin Av., Dnipropetrovs'k, Ukraine, 49005

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.
Keywords: serum proteins, cluster rhenium compounds, fluorescent spectra, electronic absorbtion spectra, secondary structure
Full text: (PDF, in Ukrainian)

References

[1] Gabbiani C. Proteins as possible targets for antitumor metal complexes: biophysical studies of their interactions–Firense: Univ. press, 2009 74 p.
[2] Marcon G., Messori L., Orioli P., Cinellu M. A., Minghetti G. Reactions of gold(III) complexes with serum albumin Eur. J. Biochem 2003 270, N 23 P. 4655–4661.
[3] Trynda-Lemiesz L., Pruchnik F. P. Studies on the interaction between human serum albumin and [Rh2(OAc)2(bpy)2(H2O)2] (OAc)2 J. Inorg. Biochem 1997 66, N 3 P. 187–192.
[4] Kratz F., Hartmann M., Keppler B., Messori L. The binding properties of two antitumor ruthenium(III) complexes to apotransferrin J. Biol. Chem 1994 269, N 4 P. 2581–2588.
[5] Stewart A. J., Blindauer C. A., Berezenko S., Sleep D., Sadler P. J. Interdomain zinc site on human albumin Proc. Natl Acad. Sci. USA 2003 100, N 7 P. 3701–3706.
[6] Carter D. C., Ho J. X. Structure of serum albumin Adv. Protein Chem 1994 45 P. 153–203.
[7] Shtemenko A. V., Collery P., Shtemenko N. I., Domasevitch K. V., Zabitskaya E. D., Golichenko A. A. Synthesis, characterization, in vivo antitumor properties of the cluster rhenium compound with GABA ligands and its synergism with cisplatin Dalton Trans 2009 N 26 P. 5132–5136.
[8] Trynda-Lemiesz L., Kozlowski H., Katsaros N. Interaction of cisand trans-RuCl2(DMSO)4 with human serum albumin Met. Based Drugs 2000 7, N 6 P. 293–299.
[9] Golichenko A. A., Shtemenko A. V., Kozhura O. V. New method of synthesis of isomers of dirhenium(III) galogenocarboxylates. Voprosy khimii i khim. tekhnologii 2001 N 6 P. 14–16.
[10] Papadopoulou A., Green R. J., Frazier R. A. Interaction of flavonoids with bovine serum albumin: a fluorescence quenching study J. Agric. Food Chem 2005 53, N 1 P. 158–163.
[11] Perez-Iratxeta C., Andrade-Navarro M. A. K2D2: estimation of protein secondary structure from circular dichroism spectra BMC Struct. Biol 2008 8 P. 25.
[12] Shtemenko O. V., Zelenyuk M. A., Shtemenko N. I., Verbytska Ya. S. The spectrophotometric investigation of interaction between rhenium complexes with phosphatidylcholine under their liposomes producing Ukr. Biokhim. Zh. 2002 74, N 6 P. 91–96.
[13] Messori L., Orioli P., Vullo D., Alessio E., Iengo E. A spectroscopic study of the reaction of NAMI, a novel ruthenium(III) anti-neoplastic complex, with bovine serum albumin Eur. J. Biochem 2000 267, N 4 P. 1206–1213.
[14] Johansson J. S. Binding of the volatile anesthetic chloroform to albumin demonstrated using tryptophan fluorescence quenching J. Biol. Chem 1997 272, N 29 P. 17961–17965.
[15] Khan M. W., Rasheed Z., Khan W., Ali R. Biochemical, biophysical and thermodynamic analysis of in vitro glycated human serum albumin Biochemistry (Mosc.) 2007 72, N 2 P. 146– 152.