## 3 Results and Discussion
### Study of the Physicochemical Properties of Aqueous IgG Colloid of Different Concentrations
Today, in pharmaceutical production, various mechanical impacts are quite often used (transfusion, stirring, vibration, shaking, etc.) [52]. We conducted a literature study and found that the most common mechanical impacts are impacts with frequencies of about 4.4 and 12 Hz. Also, modern spin chemistry methods are often used in production [21]. Installations for spin-chemical reactions that allow exposing samples to weak alternating magnetic fields usually have frequencies of the order of 8-10 Hz (frequency close to the main Schumann resonance) [53], and an integral part of the background is an alternating field with a frequency of 50 Hz, characteristic of electrical networks. Figure 3: Changes in specific electrical conductivity (**a**), molecular oxygen concentration (**b**), oxidation–reduction potential (**c**), and pH (**d**) of an aqueous colloid depending on the concentration of IgG protein molecules (M \(\pm\) SD, n = 6). *—statistically significant differences relative to samples not containing protein (_t_-test, \(p<0.05\)). Influence of Magnetic Field and Mechanical Action on the Physicochemical Properties of Aqueous IgG Colloids  
The change in the optical density of an aqueous colloid with an IgG antibody concentration of 1 mg/mL was studied after external alternating magnetic field exposure with frequencies of 8 and 50 Hz, as well as mechanical stirring with frequencies of 4.4 and 12 Hz (Figure 5a). It has been shown that the shape of the curves characterizing optical absorption remains unchanged under all influences. There is no mixing of the maxima or minima of the curves. This allows us to assert that no significant destructive processes or intense chemical reactions occur in an aqueous colloid [54]. At wavelengths greater than 330 nm, there is no significant increase in optical absorption. An increase in optical absorption in aqueous protein colloids in the longer wavelength region of the visible range is usually associated with intense processes of denaturation or aggregation [55]. In this case, the spectra differ in intensity at the optical absorption peak (\(\sim\)280-290 nm). It should be noted that in the graph, the standard deviation is shown only upward in order to avoid overlapping curves. It has been shown that statistically significant differences are observed only between groups that were inside the setup with a magnetic field with frequencies of 8 and 50 Hz. Figure 4: Three-dimensional fluorescence spectra of IgG protein after excitation at a wavelength of 240–320 nm, at different protein concentrations (mg/mL). (**A**)—10\({}^{-4}\), (**B**)—10\({}^{-6}\), (**C**)—10\({}^{-8}\), (**D**)—0. DLS measurements of hydrodynamic diameters in aqueous IgG solutions with protein concentration of 10 mg/mL are shown in Figure 5b. It has been shown that in aqueous colloids with IgG concentration of 10 mg/mL, particles with a size of \(\sim\)10 nm are observed, corresponding to individual protein molecules. In addition, a fraction with a hydrodynamic diameter of 30-50 nm is detected, corresponding to small antibody aggregates, and consisting of 30-60 protein molecules. Using the formula for the relationship between hydrodynamic radii and light scattering intensities [56], one can easily calculate that there are about 1500 individual molecules per aggregate in the colloid. Thus, we established that \(\sim\)3% of protein molecules are located in aggregates. This explains why no pronounced scattering is observed in the absorption spectrum in the long-wave region of the visible range. The shape of the size distribution changes when the aqueous protein colloid is exposed to an alternating magnetic field (8 Hz). The average size increases to 18 nm, and a significant broadening of the peak is observed. This broadening is probably explained by the fact that the \(\sim\)3% of protein molecules are located in aggregates. This is due to the fact that the \(\sim\)3% of protein molecules are located in aggregates.