Interparticle interactions and structure in nonideal solutions of human serum albumin studied by small-angle neutron scattering and Monte Carlo simulation

Osmotic Pressure, Small-Angle X-Ray, and Dynamic Light Scattering Studies of Human Serum Albumin in Aqueous Solutions

“…From the abscissa we estimate the maximal dimension within a HSA2 particle to be r max ≈ 15 nm. These results are in good agreement with small-angle neutron scattering (SANS) measurements (17,18), where the SANS data were fitted by the intensities obtained from a Monte Carlo simulation of a model system with the HSA2 molecules being approximated as hard ellipsoids of revolution with semiaxes a = 6.8 nm and b = c = 1.9 nm.…”

“…[10] For example, inserting the values of a = 6.8 nm and b = 1.9 nm, resulting from the SANS measurements for HSA2 solution (17,18), which are in fair agreement with the results of our SAXS measurements (see Fig. 6 and the discussion in the subsection SAXS results), gives the value of R H = 3.4 nm.…”

Surface enrichment of proteins at quartz/water interfaces: A neutron reflectivity study

“…If all labile hydrogens were exchanged, the sld of HSA is 3.0 × 10 −6 Å −2 . If, however, only 80% of them are exchanged (an estimate frequently used in small angle neutron scattering experiments [49][50][51]) then the sld is 2.8 × 10 −6 Å −2 . The reflectivity profiles of HSA were fitted using these two scattering densities.…”

A viscometric approach of pH effect on hydrodynamic properties of human serum albumin in the normal form

“…A conformation of HSA in the normal form is commonly approximated by an ellipsoid of revolution with one long semi-axis (a) and two shorter semi-axes (b). It appears that quite different models and values of "a" and "b" are taken by authors to interpret different experimental data (Young 1963;Peters 1985;Menon and Allen 1990;Sjöberg and Mortensen 1994;Ladam et al 2000). However, analysis of those models showed that from a hydrodynamic point of view the hydrated HSA molecules in the N-form can be treated as a prolate ellipsoid of revolution with the effective semi-axes a h = 8.2 nm and b h = 2.1 nm (Monkos 2004).…”

“…In recent years the studies mainly focus on the investigations of mechanisms of binding of HSA with different molecules and atoms, but are also directed at the determinations of the hydration, thermal stability, denaturation, interactions and other functional properties of HSA. The studies explore many different experimental techniques such as X-ray diffraction (He and Carter 1992;Olivieri and Craievich 1995;Bhattacharya et al 2000), infrared spectroscopy (Bramanti and Benedetti 1994), 1 H-NMR spectroscopy (Menon and Allen 1990;Baranowska and Olszewski 1996;Pouliquen and Gallois 2001), EPR spectroscopy (Junk et al 2011), phase-fluorometry (Buzády et al 2001), smallangle neutron scattering (Sjöberg and Mortensen 1994), electrospray mass spectrometry (Amoresano et al 1998), photon correlation spectroscopy (Sontum and Christiansen 1997), differential scanning calorimetry (Picó 1997), circular dichroism spectroscopy (Matei et al 2011), fluorescence (Vos et al 1987;Gelamo et al 2002;Kamal and Behere 2002) and viscometry (Monkos 2004). There are very few papers dealing with the influence of the pH of a solution on the physicochemical properties of HSA.…”