Abstract
The degradation of polyelectrolyte microcapsules formed on protein-free CaCO3 particles consisting of polyallylamine (PAH) and polystyrene sulfonate (PSS) and the resulting yield of protein in the presence of various salts of different concentrations, as well as at two pH values, was studied by fluorescence spectroscopy; the protein was incorporated into prepared microcapsules by adsorption. It was found that a high concentration of sodium chloride (2 M) leads to considerable dissociation of PAH, which is apparently due to the loosening of polyelectrolytes under the action of ionic strength. At the same time, 0.2 M sodium chloride and ammonium sulfate of the same ionic strength (0.1 M) exert less influence on the amount of dissociated polymer. In the case of ammonium sulfate (0.1 M), the effect is due to the competitive binding of sulfate anions to the amino groups of the polyelectrolyte. However, unlike microcapsules formed on CaCO3 particles containing protein, the dissociation of polyelectrolyte from microcapsules formed on protein-free particles increased with increasing temperature. Apparently, a similar effect is associated with the absence of a distinct shell, which was observed on microcapsules formed on protein-containing CaCO3 particles. The high level of the presence of Fluorescein isothiocyanate (FITC)-labeled Bovine Serum Albumin (BSA) in the supernatant is explained by the large amount of electrostatically bound protein and the absence of a shell that prevents the release of the protein from the microcapsules. In 2 M NaCl, during the observation period, the amount of the released protein did not exceed 70% of the total protein content in the capsules, in control samples, this value does not exceed 8%, which indicates the predominantly electrostatic nature of protein retention in capsules formed on protein-free CaCO3 particles. The increase in protein yield and peeling of PAH with increasing pH is explained by the proximity of pH 7 to the point of charge exchange of the amino group of polyelectrolyte, as a result of the dissociation of the microcapsule.
Highlights
The high level of the presence of Fluorescein isothiocyanate (FITC)-labeled Bovine Serum Albumin (BSA) in the supernatant is explained by the large amount of electrostatically bound protein and the absence of a shell that prevents the release of the protein from the microcapsules
We found that ammonium sulfate removes the effect of interaction of polyallylamine hydrochloride (PAH) with urease even at a concentration of 0.01 M [29,30]
A study was conducted to study the dissociation of polyelectrolyte microcapsules found that a high concentration of sodium chloride (2 M) leads to considerable dissociation of PAH, In thison paper, a study CaCO
Summary
Polymers 2020, 12, 520 in particular, the separation of heavy metal ions from the medium [4,6,7,8,9,10] Along with such works, which have a pronounced technical orientation, at present several researchers are actively developing the PMC in relation to the development of long-acting drugs with controlled delivery and controlled release [11,12,13,14,15]. To successfully solve such problems, it is necessary to know the dynamics of the release of encapsulated substances and the degradation of the shell. Using the example of tetramethylrhodamine isothiocyanate (TRITC)-labeled bovine serum albumin, it is shown that its yield from microcapsules depends on the number of polyelectrolyte layers of the membrane, the volume of the solution, and the method of loading the protein into microcapsules [23]
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