Nitrate Anion as a Probe for Electrostatic Interactions in Complexes Protein-Ligand
European Journal of Biophysics
Volume 1, Issue 2, April 2013, Pages: 22-27
Received: Apr. 4, 2013; Published: Jun. 10, 2013
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Smolina N. V., Research Institute for Physical Chemical Medicine, Moscow, Russia
Dobretsov G. E., Research Institute for Physical Chemical Medicine, Moscow, Russia
Syrejshchikova T. I., Lebedev Physical Institute, Moscow, Russia
Gamburg Yu. D., Frumkin Institute of Physical Chemistry and Electrochemistry, Moscow, Russia
Kalinina V. V., Research Institute for Physical Chemical Medicine, Moscow, Russia
Gryzunov Yu. A., Research Institute for Physical Chemical Medicine, Moscow, Russia
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We are proposing a new technique for studying interaction of charged biomolecules. It is based on a difference between nitrate and chloride anion influence on electrostatic interactions in order to detect the role of positively charged guanidine groups of proteins. This comparison was demonstrated for human serum albumin (HSA) interaction with a fluorescent reporter, CAPIDAN. Nitrate anions lower their binding constant (K). There are two causes that are responsible for that K decrease induced by nitrate. The first, rise of the ionic strength (like to chloride), and the second, a specific one: at the same concentration and ionic strength nitrate anion more significantly lowers K than chloride anion. The study of electric conductivity of chloride and nitrate salts shows that nitrate anions better than chloride anions form complexes with gu-anidine cations. Therefore it can be assumed that the nitrate-chloride techniques detect a direct contact of negatively charged carboxyl of CAPIDAN with positively charged arginine residues of HSA. HSA site I includes Arg 218 and Arg 222. It is possible that the CAPIDAN carboxyl binds to one of these arginines.
Human Serum Albumin, Drug-Binding Site, Ngatively Charged Ligands, Nitrate Anion Blocking Arginine Charge, Fluorescent Probe CAPIDAN
To cite this article
Smolina N. V., Dobretsov G. E., Syrejshchikova T. I., Gamburg Yu. D., Kalinina V. V., Gryzunov Yu. A., Nitrate Anion as a Probe for Electrostatic Interactions in Complexes Protein-Ligand, European Journal of Biophysics. Vol. 1, No. 2, 2013, pp. 22-27. doi: 10.11648/j.ejb.20130102.12
I.M. Klotz, "Spectrophotometric investigation of the inte-ractions of proteins with organic anions", J. Amer. Chem. Soc, vol. 68, pp. 2299-2304, November 1946.
I.M. Klotz, R. "Burkhard and J. Urkuhart, "Structural speci-ficities in the interactions of some organic ions with serum albumin", J. Amer. Chem. Soc., vol. 74, pp. 202-208, 1952.
G.E. Dobretsov, B. Polyak, N. Smolina, T. Babushkina, T. Syrejshchikova, T. Klimova, V. Sverbil, A. Peregudov, Yu. Gryzunov, and O. Sarkisov, "Interaction of a fluorescent probe, CAPIDAN, with human serum albumin", J. Photochem. Photobiol. A: Chemistry, vol. 251, pp. 134-140, January 2013.
Yu.A. Gryzunov and G.E. Dobretsov, "Natural conformation of human serum albumin and its changes in pathology", in Protein Conformation: New Research, Ed. L.B. Roswell. Nova Publishers, New York, 2008, pp. 125-159.
D.R. Sellers and G.A. Ghiron, "Role of the tryptophan fluo-rescent state in the ultraviolet-induced inactivation of be-ta-trypsin", Photochem. Photobiol., vol. 18, pp. 393-402, 1973.
D.B. Calhoun, J.M. Vanderkooi, G.R. Holtorn, and nS.W. Englander, "Protein fluorescence quenching by small mole-cules: protein penetration versus solvent exposure", Proteins: Structure, Function, and Genetics, vol. 1(2), pp. 109-115, October 1986.
N.V. Smolina, Yu.A. Gryzunov, N.M. Maximova, G.E. Do-bretsov, M.G. Uzbekov, E.Yu. Misionzhnik, and O.P. Verto-gradova, "Characteristics of albumin molecule binding centers in patients with anxious depression. Study by the fluorescence quenching method", Bull. Exp. Biol. Med., vol. 144(5), pp. 674-676, November 2007 [Bull. Exp. Biol. Med., vol. 144(11), p. 514, 2007].
T.I. Syrejshchikova, Yu.A. Gryzunov, N.V. Smolina, A.A. Komar, M.G. Uzbekov, E.Yu. Misionzhnik, and N.M. Mak-simova, "Subnanosecond fluorescent spectroscopy of human serum albumin as a method for estimation of depression therapy efficiency", Laser Physics, vol. 20, pp. 1074-1078, November 2010.
S.M. Andrade, S.M. Costa, J.W. Borst, A. van Hoek, and A.J. Visser, "Translational and rotational motions of albumin sensed by a non-covalent associated porphyrin under physiological and acidic conditions: a fluorescence correlation spectroscopy and time resolved anisotropy study", J. Fluoresc., vol. 18, pp. 601-610, May-July 2008.
M. Banerjee, U. Pal, A. Subudhhi, A. Chakrabarti, and S. Basu, "Interaction of Merocyanine 540 with serum albumins: photophysical and binding studie", J. Photochem. Photobiol. B, vol. 108, pp. 23-33, March 2012.
P. Bolel, N. Mahapatra, and M. Halder, "Optical spectroscopic exploration of binding of Cochineal Red A with two homologous serum albumins", J. Agric. Food. Chem., vol. 60, pp. 3727-3734, April 2012.
O. Stern and M. Volmer, „Über die Abklingzeit der Fluores-zenz", Physikalische Zeitschrift, vol. 20, pp. 183-188, 1919.
J.R. Lakowicz, Principles of Fluorescence Spectroscopy, Springer, 2006, p. 256.
G.E. Dobretsov, T. I. Syreishchikova, Yu. A. Gryzunov, N. V. Smolina, and A. A. Komar, "Features of the binding of the fluorescent probe K-35 to albumin", Biophysics , vol. 55, , pp. 182–187, March-April 2010.
G.E. Dobretsov, T.I. Syreishchikova, and N.V. Smolina, "Molecular mobility of a fluorescent probe in binding sites of an albumin molecules", Biophysics, vol. 56, pp. 403–406, May-June 2011.
U. Kragh-Hansen, V.T.G. Chang, and M. Otagiri, "Practical aspects of the ligand-binding and enzymatic properties of human serum albumin", Biol. Pharm. Bull., vol. 25, pp. 695–704, June 2002.
J. Ghuman, P.A. Zunszain, I. Petitpas, A.A. Bhattacharya, M. Otagiri, and S.Curry, "Structural basis of the drug-binding specificity of human serum albumin", J. Mol. Biol., vol. 353, pp. 38-52, October 2005.
V.T. Chuang and M. Otagiri, "Stereoselective binding of human serum albumin", Chilarity, vol. 18(93), pp. 159-166, February 2006.
Handbook of Chemistry and Physics, Ed. D.R. Line, CRC Press, 2001.
T. Shimizu, „Chemical components of firework compositions", in: K. Kosanke, B. Kosanke, I. von Maltitz, T. Shimizu, M. A. Wilson, N. Kubota, C. Jennings-White, D. Chapman, Pyrotechnic Chemistry, 2004, p.30.
M.A. Kiselev, Yu.A. Gryzunov, G.E. Dobretsov, and M.N. Komarova, "The size of human serum albumin molecules in solution", Biophysics, vol. 46, pp. 402-405, 2001.
E.L. Gelamo, R. Itri, A. Alonso, J.V. da Silva, and M. Tabak, "Small-angle X-ray scattering and electron paramagnetic resonance study of the interaction of bovine serum albumin with ionic surfactants", J. Colloid Interface Sci., vol. 277, pp. 471- 482, September 2004.
Watanabe H., Kragh-Hansen U., Tanase S., Nakajou K., Mitarai M., Iwao Y., Maruyama T., and Otagiri M. "Con-formational stability and warfarin-binding properties of human serum albumin studied by recombinant mutants", Biochem. J., vol. 357 (Pt 1), pp. 269-274, July 2001.
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