Interaction of Serum Albumin and Fatty Acid Molecules with Graphenes of Shungite Carbon Nanoparticles in Aqueous Dispersion Assessed by Raman Spectroscopic Analysis of Water in the High Wavenumber Region

Rozhkov, S. S.; Goryunov, A. S.; Kolodey, Vladimir; Pron’kina, L. A.; Rozhkova, N. N.

doi:10.1134/s0006350922060203

Cited by 2 publications

(4 citation statements)

References 22 publications

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“…A study of the colloidal stability of albumin dispersions using Raman scattering in the wavenumber range 3000–3600 cm −1 was carried out in [ 87 , 88 ]. Analysis of spectral lines in this range, caused by OH stretching vibrations in the network of hydrogen bonds of water, showed the important role of the network in the supramolecular organization (formation of dynamic clusters) of protein dispersion.…”

Section: Resultsmentioning

confidence: 99%

“…In the concentration range of 0.1–0.3 mg/mL of protein, the defects are filled, and the system of hydrogen bonds is stabilized to the greatest extent. The destabilization of the hydrogen bond system with further increasing protein concentration is attributed to its association [ 87 , 88 ], the degree of which was estimated from the data of the DLS method.…”

Section: Resultsmentioning

confidence: 99%

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Molecular Serum Albumin Unmask Nanobio Properties of Molecular Graphenes in Shungite Carbon Nanoparticles

Rozhkov,

Goryunov,

Rozhkova

2024

IJMS

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Serum albumin is a popular macromolecule for studying the effect of proteins on the colloidal stability of nanoparticle (NP) dispersions, as well as the protein–nanoparticle interaction and protein corona formation. In this work, we analyze the specific conformation-dependent phase, redox, and fatty acid delivery properties of bovine albumin in the presence of shungite carbon (ShC) molecular graphenes stabilized in aqueous dispersions in the form of NPs in order to reveal the features of NP bioactivity. The formation of NP complexes with proteins (protein corona around NP) affects the transport properties of albumin for the delivery of fatty acids. Being acceptors of electrons and ligands, ShC NPs are capable of exhibiting both their own biological activity and significantly affecting conformational and phase transformations in protein systems.

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Section: Resultsmentioning

confidence: 99%

Section: Resultsmentioning

confidence: 99%

Molecular Serum Albumin Unmask Nanobio Properties of Molecular Graphenes in Shungite Carbon Nanoparticles

Rozhkov,

Goryunov,

Rozhkova

2024

IJMS

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“…This is not surprising, since the cluster structure of ordinary water is one of the most difficult problems of modern science [28]. In this case, the system of hydrogen bonds can determine and regulate the balance of forces, promoting either the disaggregation or complex formation of components, depending on the presence and state of defects in the water structure [29]. Dissolved components can affect the network of hydrogen bonds in water, being located in its defects.…”

Section: Introductionmentioning

confidence: 99%

“…When studying the state of water hydrogen bonds in SA dispersions by Raman spectroscopy in the range of 3200-3600 cm −1 , we obtained data [29] where self-association of protein molecules and formation of their clusters were accompanied by a change in the ordering of hydrogen bonds. An earlier [31] structuring of interfacial water on silica surface studied by the sum frequency generation (SFG) vibrational spectroscopy was observed.…”

Section: Introductionmentioning

confidence: 99%

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

et al. 2023

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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 studiedin 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.

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Interaction of Serum Albumin and Fatty Acid Molecules with Graphenes of Shungite Carbon Nanoparticles in Aqueous Dispersion Assessed by Raman Spectroscopic Analysis of Water in the High Wavenumber Region

Cited by 2 publications

References 22 publications

Molecular Serum Albumin Unmask Nanobio Properties of Molecular Graphenes in Shungite Carbon Nanoparticles

Molecular Serum Albumin Unmask Nanobio Properties of Molecular Graphenes in Shungite Carbon Nanoparticles

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

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