Calculation of the Effective Macromolecular Radii of Human Serum Albumin from the Shear Viscosity Data for Its Aqueous Solutions

  • O. V. Khorolskyi V.G. Korolenko National Pedagogical University of Poltava
Keywords: human serum albumin, aqueous solution, effective macromolecular radius, Malomuzh–Orlov theory


The Malomuzh–Orlov theory is used to analyze the experimental shear viscosity data obtained for aqueous solutions of human serum albumin (HSA) at pH = 7.0 in wide temperature and concentration intervals, which allowed the effective radii of HSA macromolecules to be calculated. It is shown that three intervals of the effective molecular radius of HSA with different behaviors can be distinguished in a temperature interval of 278–318 K: 1) below the crossover concentration, the effective molecular radius of HSA remains constant; 2) in the interval from the crossover concentration to about 10 wt%, the effective molecular radius of HSA in the aqueous solution nonlinearly decreases; and 3) at concentrations of 10.2–23.8 wt%, the effective radius of HSA macromolecules linearly decreases, as the concentration grows. The assumption is made that the properties of water molecules in the solution bulk play a crucial role in the dynamics of HSA macromolecules at the vital concentrations of HSA in the solutions. The role of water near the surface of HSA macromolecules and the corresponding changes of its physical properties have been discussed.


L.M. Tarasenko, K.S. Neporada, V.K. Grygorenko. Functional Biochemistry (Poltava, 2000) (in Ukrainian).

L.O. Kovalkina, G.I. Moroz. Albumin as a polyfunctional drug. Ukr. Zh. Extrem. Med. 11, 18 (2010) (in Ukrainian).

Yu.V. Khmelevskii, O.K. Usatenko. Main Biochemical Constants of Human in Health and Disease (Zdorov’ya, 1987) (in Russian).

T. Peters, jr. All About Albumin: Biochemistry, Genetics, and Medical Applications (Academic Press, 1996).

X.M. He, D.C. Carter. Atomic structure and chemistry of human serum albumin. Nature 3582, No. 6383, 209 (1992).

B. Sj¨oberg, K. Mortensen. Interparticle interactions and structure in nonideal solutions of human serum albumin studied by small-angle neutron scattering and Monte Carlo simulation. Biophys. Chemist. 52, 131 (1994).

M.L. Ferrer, R. Duchowicz, B. Carrasco, J.G. de la Torre, A.U. Acu˜na. The conformation of serum albumin in solution: A combined phosphorescence depolarization-hydrodynamic modeling study. Biophys. J. 80, 2422 (2001).

P.C. Sontum, C. Christiansen. Photon correlation spectroscopy applied to characterization of denaturation and thermal stability of human albumin. J. Pharm. Biomed. Anal. 16, 295 (1997).

A. Amoresano, A. Andolfo, R.A. Siciliano, R. Cozzolino, L. Minchiotti, M. Galliano, P. Pucci. Analysis of human serum albumin variants by mass spectrometric procedures. Biochim. Biophys. Acta 1384, 79 (1998).

D. Pouliquen, Y. Gallois. Physicochemical properties of structured water in human albumin and gammaglobulin solutions. Biochimie 83, 891 (2001).

J.K.A. Kamal, D.V. Behere. Spectroscopic studies on human serum albumin and methemalbumin: Optical, steady-state, and picosecond time–resolved fluorescence studies, and kinetics of substrate oxidation by methemalbumin. J. Biol. Inorg. Chem. 7, 273 (2002).

K. Monkos. On the hydrodynamics and temperature dependence of the solution conformation of human serum albumin from viscometry approach. Biochim. Biophys. Acta 1700, 27 (2004).

N.P. Malomuzh, E.V. Orlov. Static shear viscosity of a bimodal suspension. Ukr. J. Phys. 50, 618 (2005).

E.V. Orlov. Shear viscosity of dispersions of particles with liquid shells. Colloid J. 72, 820 (2010).

O.V. Khorolskyi. Effective radii of macromolecules in dilute polyvinyl alcohol solutions. Ukr. J. Phys. 63, 144 (2018).

O.V. Khorolskyi. Viscometric research of concentration regimes for polyvinyl alcohol solutions. Ukr. Fiz. Zh. 60, 882 (2015) (in Ukrainian).

L.A. Bulavin, N.P. Malomuzh. Dynamic phase transition in water as the most important factor in provoking protein denaturation in warm-blooded organisms. Fiz. Zhivogo 18, 16 (2010) (in Russian)

A.I. Fisenko, N.P. Malomuzh. To what extent is water responsible for the maintenance of the life for warm-blooded organisms? Int. J. Mol. Sci. 10, 2383 (2009)

Yu.I. Khurgin. Hydration of globular proteins. Zh. Vsesoyuz. Khim. Obshsch. 21, 684 (1976) (in Russian)

A.B. Kurzaev, V.I. Kvlividze, V.F. Kiselev. Specific character of water phase transition on the surface of biological and inorganic dispersed bodies at low temperatures. Svyaz. Voda Disp. Syst. 4, 156 (1977) (in Russian)

V.Ya. Volkov, B.V. Sakharov, L.A. Volkova. Radiospectroscopic methods in cryobiology. Kriobiologiya 4, 3 (1985) (in Russian)

T.V. Lokotosh, N.P. Malomuzh, V.L. Zakharchenko. The relationship between the water structure and the anomalies of water density and dielectric constant. Zh. Strukt. Khim. 44, 1085 (2003) (in Russian)

L.A. Bulavin, N.P. Malomuzh, K.N. Pankratov. Self-diffusion in water. J. Struct. Chem. 47, Suppl. 1, S50 (2006).

How to Cite
Khorolskyi, O. (2019). Calculation of the Effective Macromolecular Radii of Human Serum Albumin from the Shear Viscosity Data for Its Aqueous Solutions. Ukrainian Journal of Physics, 64(4), 287.
Physics of liquids and liquid systems, biophysics and medical physics