Behavior of proteins alone and upon interactions with nanosilicas and polymers in aqueous media

V.M. Gun’ko

doi:10.15407/hftp17.03.283

Authors

V.M. Gun’ko Chuiko Institute of Surface Chemistry of National Academy of Sciences of Ukraine https://orcid.org/0000-0001-6333-3441

DOI:

https://doi.org/10.15407/hftp17.03.283

Keywords:

protein solution, nanosilica, protein/nanosilica, protein/polymer/nanosilica, aggregation, dynamic light scattering, aqueous dispersion behavior

Abstract

The structural, conformational, interfacial, aggregation, and temperature behaviors of proteins dissolved alone or upon interactions with nanosilica (NS) or NS/polymers in aqueous media depend on numerous factors: type, structure, and concentration of proteins, solution pH, ionic strength, temperature, concentrations of solutes (e.g., polymers) and solid particles (e.g., nanooxides), various external actions such as heating, cooling, sonication, mixing, high-frequency emission (HFE), sample prehistory, etc. Features and control of the protein behavior in complex dispersions are of interest from a practical point of view because similar systems are widely used in medicine, biotechnology, pharmindustry, and food industry. To elucidate some aspects of dependences of the nanostructured dispersion characteristics on the mentioned factors, several proteins (bovine serum albumin, BSA, ovalbumin, OVA, fibrinogen, Fg, Fg parts (central E (FE) and end D (FN) domains), and a₂–macroglobulin, MG), two NS (A–300 and A–50), and three polymers (poly(vinyl alcohol), PVA, poly(vinyl pyrrolidone), PVP, and poly(ethylene glycol), PEG) have been used in dynamic light scattering (DLS) investigations of the aqueous solutions and suspensions. Changes in the protein concentrations (1–10 wt. %) relatively weakly affect the particles size distributions (PSD) of BSA in contrast to OVA strongly disaggregated with concentration due to changes in the intermolecular interactions between supramolecular structures. This effect depends also on the viscosity (h) that could give apparent changes in PSD without corrections in the h values upon the treatment of autocorrelation functions. To avoid this effect, mainly diluted dispersions have been studied. The heating/cooling effects, as well as HFE (resulting in certain heating of the dispersions and certain changes in the hydrogen bonding), depend on the type (molecular shapes) and size of proteins, and they are maximal for nonglobular Fg (long large molecules) in comparison to smaller (FE, FN) or globular (BSA, OVA, MG) proteins. Features of protein interactions with NS and NS/polymer depend on the NS type (A–300 or A–50) and the presence of the OH groups in bound polymers (PVA) since the OH groups provide stronger interactions and aggregations with proteins than other studied polymers without the OH groups in the chains (PEG, PVP). As a whole, the obtained results show possible pathways to control the behavior of the protein containing dispersions in a wide range of the characteristics.

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