The Role of Water Hydrogen Bonds in the Formation of Associates and Condensates in Dispersions of Serum Albumin with Shungite Carbon and Quartz Nanoparticles

Author:

Rozhkov Sergey1,Goryunov Andrey1ORCID,Kolodey Vladimir2,Pron’kina Lyubov2,Rozhkova Natalia2ORCID

Affiliation:

1. Institute of Biology, Karelian Research CentreRAS, 185910 Petrozavodsk, Russia

2. Institute of Geology, Karelian Research Centre RAS, 186910 Petrozavodsk, Russia

Abstract

The role of the network of water hydrogen bonds in the regulation of the intermolecular interaction’s responsible for colloidal stability of dispersions has been studied in order to search for general patterns of interaction between water, nanoparticles, and bio-macromolecules. Raman spectroscopy for mixed dispersions of bovine serum albumin (SA), shungite carbon nanoparticles (ShC NPs), and quartz nanoparticles (quartz NPs) was performed within the wave number range 3200–3600 cm−1. The main spectral lines in this range are caused by the OH stretch vibrations of water molecules. We analyzed the state of the water hydrogen bonding network for dispersions of varied ratios of both fatty acid-containing and fatty acid-free SA macromolecules, ShC NPs, and silica NPs in the range 0.01–10 mg/mL.We used dynamic light scattering to control the sizes of the protein associates and protein associates with ShC NPs and quartz NPs. The strength of the hydrogen bonds in water depends essentially non-linearly, but in a qualitatively similar way, on the concentrations of the dispersion components. The initial strengthening of the bonds is followed by their loosening with a further increase in the concentration of the components. This is accompanied by the association of the dispersion components. We estimate the thickness of the protein corona layer as 20–25 nm for ShC NPs and 28–33 nm for quartz NPs, depending on the SA concentration. Colloidal stability of the aqueous dispersion is determined almost completely by an association of the protein with NPs. In contrast, colloidal stability of a pure protein solution is regulated by the formation of protein clusters of two main types and sizes. The association effects of SA with ShC NPs are evident in microscopic images of condensate films. The structures differ significantly for native and fatty acid-free SA in shape and size.

Funder

Framework of State Order Projects

Publisher

MDPI AG

Subject

Materials Chemistry,Surfaces, Coatings and Films,Surfaces and Interfaces

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