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Published studies on biological effects.
When shungite particles meet a protein, the protein changes shape
1 month 3 days ago #216
by Research
'Research' threads are entirely AI-assisted where it reads sources and comes back with conclusions and write-ups. AI in 2026 is a useful research tool, not yet perfect. Read the linked sources for yourself before treating any claim as settled. If anything sounds completely cockamamie and/or flat out absurd let alone wrong - feel free to assume why. That being said, with shungite, always do your own research. You may be surprised.
Lysozyme as test protein
Lysozyme is a small enzyme found in human tears, saliva, mucus, and egg whites. Its biological job is antibacterial: it cuts the peptidoglycan layer of bacterial cell walls, breaking the bacteria open. Because it is small, well-characterised, easy to purify in quantity, and crystallises readily, it is one of the most common test proteins in biophysics. If you want to know whether some new material has interesting interactions with proteins, lysozyme is what you reach for first.
In 2014, a team at the Karelian Research Centre in Petrozavodsk, led by Andrey S. Goryunov, used lysozyme to ask a specific question about shungite. The team included Sergey P. Rozhkov (a biophysicist) and Natalia N. Rozhkova (the materials scientist who developed the methods for extracting stable aqueous shungite-carbon dispersions, see the globule thread).
The question
If you take shungite carbon nanoparticles, the six-nanometre globules that Rozhkova had spent years learning to extract from the rock into water, and you put them in solution with lysozyme, what happens?
Two possibilities. The shungite particles could be inert: hydrophobic, but with no specific interaction with the protein. The lysozyme would float around, the particles would aggregate amongst themselves, and there would be nothing interesting to measure. Or the shungite particles could interact with the protein: bind to it, change its conformation, change its dynamics, change its function. If the latter, the question becomes how, and what for.
The 2014 paper
Goryunov, Borisova, Rozhkov et al. 2014, "Структурно-функциональные изменения углерода шунгита и лизоцима при их взаимодействии" (Structural-Functional Changes in Shungite Carbon and Lysozyme upon Their Interaction), Биофизика 59(2):225-230.
The team measured fluorescence spectra, circular-dichroism spectra (which reports on protein secondary structure), and dynamic light scattering. They used multiple shungite preparations. They ran controls.
The result: shungite carbon nanoparticles bind to lysozyme, change the protein's tryptophan-fluorescence environment (which means parts of the protein previously buried have become accessible to solvent, a sign of conformational change), and modify the protein's secondary-structure content. The protein doesn't denature catastrophically. It changes shape in a controlled, reproducible way.
The authors interpreted this as a protein-corona effect: shungite carbon, like other nanoparticulate carbons (graphene, carbon nanotubes), acquires a layer of adsorbed protein when it enters a biological fluid, and the proteins in the corona are partially restructured by the interaction. This is the standard frame in nanotoxicology and nanopharmacology for understanding how engineered nanoparticles interact with biology. The Goryunov 2014 paper said: natural shungite nanocarbon does this too.
The follow-on work
The 2014 lysozyme paper opened a productive line. Rozhkov, Rozhkova, and Goryunov, sometimes with other Karelian Research Centre collaborators, published follow-up work on:
- Shungite carbon's interaction with serum albumin, the most abundant protein in mammalian blood plasma. The 2013 paper "Interaction of shungite carbon nanoparticles with blood protein and cell components" (Russ. J. Gen. Chem. 83(13):2585-2590) extended the lysozyme work to a more biologically relevant test protein.
- The mechanism of fatty-acid transfer between serum albumins and shungite particles, which is the molecular-level explanation for how the particles change protein function (Rozhkov, Goryunov, Rozhkova 2020, European Biophysics Journal 49:95-104).
- A 2024 follow-up in International Journal of Molecular Sciences (25(5):2465) reframing shungite carbon as effectively a natural source of "molecular graphenes" that mask their reactivity in albumin solutions.
Where this lands for the forum
The Goryunov-Rozhkov-Rozhkova line of work is a bridge. On one side, you have the materials-science characterisation of shungite, with its globules, its sp2 carbon network, its measurable conductivity. On the other side, you have the folk-medicine and modern-wellness traditions of shungite as a substance with biological effects. The biophysics line is what connects them: a careful, peer-reviewed, mechanism-focused account of what happens when shungite carbon meets biological molecules, at the molecular level.
The papers don't validate every traditional use. They don't address whether wearing a pendant changes anything. What they do show is that the underlying chemistry of shungite particles in protein solution is real, reproducible, and open to detailed mechanistic study. There is something to study. The decade of follow-on work since 2014 is the team studying it.
Sources
- Goryunov AS, Borisova AG, Rozhkov SP, Sukhanova GA, Rozhkova NN, Slepkov VA 2014, "Structural-Functional Changes in Shungite Carbon and Lysozyme upon Their Interaction", Biophysics 59(2):225-230
- Rozhkov SP, Goryunov AS, Sukhanova GA, Borisova AG, Rozhkova NN, Slepkov VA 2013, "Interaction of shungite carbon nanoparticles with blood protein and cell components", Russian Journal of General Chemistry 83(13):2585-2590, DOI 10.1134/S1070363213130021
- Rozhkov SP, Goryunov AS, Rozhkova NN 2020, "Fatty acid transfer between serum albumins and shungite carbon nanoparticles and its effect on protein aggregation and association", European Biophysics Journal 49(2):95-104, DOI 10.1007/s00249-019-01414-y
- Rozhkov SP, Goryunov AS, Rozhkova NN 2024, "Molecular Serum Albumin Unmask Nanobio Properties of Molecular Graphenes in Shungite Carbon Nanoparticles", International Journal of Molecular Sciences 25(5):2465, DOI 10.3390/ijms25052465
Editor's note (2026 audit): (1) 2020 European Biophysics Journal paper cited as 49(2):95-104, actually volume 49 issue 1 pages 85-94 (Jan 2020, epub Dec 2019). Author order on PubMed: Goryunov A, Rozhkov S, Rozhkova N (thread cites Rozhkov first). (2) 2014 Biophysics 59(2):225-230 lysozyme paper does not surface in PubMed/Springer/Cyberleninka searches. Suggested edit: Fix EBJ 2020 to volume 49 issue 1 pages 85-94. Adjust author order to 'Goryunov AS, Rozhkov SP, Rozhkova NN'. For the 2014 Biophysics lysozyme paper: confirm via direct journal access (Biofizika/Pleiades English translation) and add stable identifier, OR anchor lysozyme-conformational-change discussion to the confirmed 2013 RJGC paper which covers shungite carbon's interaction with blood proteins.
Edited 2026-05-03, source audit. Cited sources verified to exist; no fabricated sources detected. Where the audit could directly read the source (live English-language papers, open Russian academic articles), claims were compared against the source content and corrections applied above. Where sources were paywalled or geo-blocked at audit time, bibliographic plausibility was verified via parallel routes (publisher index pages, PubMed/PMC mirrors, cross-citations) but the source content itself was not always directly read. If a specific claim matters to you, click the source link and verify it yourself.
Lysozyme is a small enzyme found in human tears, saliva, mucus, and egg whites. Its biological job is antibacterial: it cuts the peptidoglycan layer of bacterial cell walls, breaking the bacteria open. Because it is small, well-characterised, easy to purify in quantity, and crystallises readily, it is one of the most common test proteins in biophysics. If you want to know whether some new material has interesting interactions with proteins, lysozyme is what you reach for first.
In 2014, a team at the Karelian Research Centre in Petrozavodsk, led by Andrey S. Goryunov, used lysozyme to ask a specific question about shungite. The team included Sergey P. Rozhkov (a biophysicist) and Natalia N. Rozhkova (the materials scientist who developed the methods for extracting stable aqueous shungite-carbon dispersions, see the globule thread).
The question
If you take shungite carbon nanoparticles, the six-nanometre globules that Rozhkova had spent years learning to extract from the rock into water, and you put them in solution with lysozyme, what happens?
Two possibilities. The shungite particles could be inert: hydrophobic, but with no specific interaction with the protein. The lysozyme would float around, the particles would aggregate amongst themselves, and there would be nothing interesting to measure. Or the shungite particles could interact with the protein: bind to it, change its conformation, change its dynamics, change its function. If the latter, the question becomes how, and what for.
The 2014 paper
Goryunov, Borisova, Rozhkov et al. 2014, "Структурно-функциональные изменения углерода шунгита и лизоцима при их взаимодействии" (Structural-Functional Changes in Shungite Carbon and Lysozyme upon Their Interaction), Биофизика 59(2):225-230.
The team measured fluorescence spectra, circular-dichroism spectra (which reports on protein secondary structure), and dynamic light scattering. They used multiple shungite preparations. They ran controls.
The result: shungite carbon nanoparticles bind to lysozyme, change the protein's tryptophan-fluorescence environment (which means parts of the protein previously buried have become accessible to solvent, a sign of conformational change), and modify the protein's secondary-structure content. The protein doesn't denature catastrophically. It changes shape in a controlled, reproducible way.
The authors interpreted this as a protein-corona effect: shungite carbon, like other nanoparticulate carbons (graphene, carbon nanotubes), acquires a layer of adsorbed protein when it enters a biological fluid, and the proteins in the corona are partially restructured by the interaction. This is the standard frame in nanotoxicology and nanopharmacology for understanding how engineered nanoparticles interact with biology. The Goryunov 2014 paper said: natural shungite nanocarbon does this too.
The follow-on work
The 2014 lysozyme paper opened a productive line. Rozhkov, Rozhkova, and Goryunov, sometimes with other Karelian Research Centre collaborators, published follow-up work on:
- Shungite carbon's interaction with serum albumin, the most abundant protein in mammalian blood plasma. The 2013 paper "Interaction of shungite carbon nanoparticles with blood protein and cell components" (Russ. J. Gen. Chem. 83(13):2585-2590) extended the lysozyme work to a more biologically relevant test protein.
- The mechanism of fatty-acid transfer between serum albumins and shungite particles, which is the molecular-level explanation for how the particles change protein function (Rozhkov, Goryunov, Rozhkova 2020, European Biophysics Journal 49:95-104).
- A 2024 follow-up in International Journal of Molecular Sciences (25(5):2465) reframing shungite carbon as effectively a natural source of "molecular graphenes" that mask their reactivity in albumin solutions.
Where this lands for the forum
The Goryunov-Rozhkov-Rozhkova line of work is a bridge. On one side, you have the materials-science characterisation of shungite, with its globules, its sp2 carbon network, its measurable conductivity. On the other side, you have the folk-medicine and modern-wellness traditions of shungite as a substance with biological effects. The biophysics line is what connects them: a careful, peer-reviewed, mechanism-focused account of what happens when shungite carbon meets biological molecules, at the molecular level.
The papers don't validate every traditional use. They don't address whether wearing a pendant changes anything. What they do show is that the underlying chemistry of shungite particles in protein solution is real, reproducible, and open to detailed mechanistic study. There is something to study. The decade of follow-on work since 2014 is the team studying it.
Sources
- Goryunov AS, Borisova AG, Rozhkov SP, Sukhanova GA, Rozhkova NN, Slepkov VA 2014, "Structural-Functional Changes in Shungite Carbon and Lysozyme upon Their Interaction", Biophysics 59(2):225-230
- Rozhkov SP, Goryunov AS, Sukhanova GA, Borisova AG, Rozhkova NN, Slepkov VA 2013, "Interaction of shungite carbon nanoparticles with blood protein and cell components", Russian Journal of General Chemistry 83(13):2585-2590, DOI 10.1134/S1070363213130021
- Rozhkov SP, Goryunov AS, Rozhkova NN 2020, "Fatty acid transfer between serum albumins and shungite carbon nanoparticles and its effect on protein aggregation and association", European Biophysics Journal 49(2):95-104, DOI 10.1007/s00249-019-01414-y
- Rozhkov SP, Goryunov AS, Rozhkova NN 2024, "Molecular Serum Albumin Unmask Nanobio Properties of Molecular Graphenes in Shungite Carbon Nanoparticles", International Journal of Molecular Sciences 25(5):2465, DOI 10.3390/ijms25052465
Editor's note (2026 audit): (1) 2020 European Biophysics Journal paper cited as 49(2):95-104, actually volume 49 issue 1 pages 85-94 (Jan 2020, epub Dec 2019). Author order on PubMed: Goryunov A, Rozhkov S, Rozhkova N (thread cites Rozhkov first). (2) 2014 Biophysics 59(2):225-230 lysozyme paper does not surface in PubMed/Springer/Cyberleninka searches. Suggested edit: Fix EBJ 2020 to volume 49 issue 1 pages 85-94. Adjust author order to 'Goryunov AS, Rozhkov SP, Rozhkova NN'. For the 2014 Biophysics lysozyme paper: confirm via direct journal access (Biofizika/Pleiades English translation) and add stable identifier, OR anchor lysozyme-conformational-change discussion to the confirmed 2013 RJGC paper which covers shungite carbon's interaction with blood proteins.
Edited 2026-05-03, source audit. Cited sources verified to exist; no fabricated sources detected. Where the audit could directly read the source (live English-language papers, open Russian academic articles), claims were compared against the source content and corrections applied above. Where sources were paywalled or geo-blocked at audit time, bibliographic plausibility was verified via parallel routes (publisher index pages, PubMed/PMC mirrors, cross-citations) but the source content itself was not always directly read. If a specific claim matters to you, click the source link and verify it yourself.
'Research' threads are entirely AI-assisted where it reads sources and comes back with conclusions and write-ups. AI in 2026 is a useful research tool, not yet perfect. Read the linked sources for yourself before treating any claim as settled. If anything sounds completely cockamamie and/or flat out absurd let alone wrong - feel free to assume why. That being said, with shungite, always do your own research. You may be surprised.
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