Last year when Nicolas Hulscher said that McCairn found "amyloid fibrils" in the 3-year-old's blood, Ian Musgrave replied: "That's a cellulose fibre, not amyloid." [https://x.com/KevinMcCairnPhD/status/1959430726237168121] Then McCairn said: "No it isn't. It's amyloidogenic fibrin." And Musgrave said: "No, it is not. It's just a cellulose fibre. I've EMed enough real amyloids and sighted enough cellulose fibres under the microscope to know which is which." And Musgrave said: "Thioflavin will stain almost anything if you don't use the right conditions, I have long experience with thioflavin and amyloids."
Then McCairn said: "No it doesn't when used at the right molar concentration, coupled with use of microinjection techniques to target the object. Besides cellulose doesn't auto-fluoresce. If you think it cellulose why don't recapitulate the slide with the fibrous clot being in-situ with the blood layer, and with connecting micro clot globular forms connecting each ends."
What he called the "globular forms" connected to the ends of the fiber were some random blobs on the slide that didn't even look connected to the fiber, and I don't think McCairn even verified if the blobs were made of fibrin or not. [https://sars2.net/clot3.html#Substack_post_about_SEM_images_of_the_3_year_olds_fiber] And McCairn forgot to mention that cellulose can be strongly fluorescent if it has been bleached white.
McCairn then replied that in order to eliminate false positives, "I run antibodies, use SEM/EDX, and Raman on samples". [https://x.com/KevinMcCairnPhD/status/1959414465293959358] I have told him to verify that his fibers are actually made of fibrin by doing either immunostaining with anti-fibrin antibodies or Raman spectroscopy, but I haven't seen him ever actually publish the results of either type of analysis (even though I don't know if by antibodies he meant anti-fibrin antibodies or antibodies to recognize amyloid proteins).
Last year McCairn published two Substack posts about the 3-year-old's fiber. In the first post he showed light microscope images of the sample, and he indicated that he was next going to run SEM, EDX, and Raman on the sample. [https://substack.com/@kevinwmccairnphd282302/p-164383206] In the second post he posted SEM images of the sample but he didn't describe EDX or Raman results. When I asked him why he didn't publish the EDX or Raman results, he responded to me by doing a stream where he showed the EDX results, but he said that he couldn't do Raman "because the sample was sent on a glass slide, and you need quartz slides for Raman". [https://x.com/KevinMcCairnPhD/status/1961314002304438763] But then I pointed out that McCairn had earlier said that the sample was preserved for Raman, and a glass slide may have been acceptable for Raman according to LLMs. And he already knew in advance that the sample was on a glass slide, so why did he even say he was going to do Raman?
I still suspect that he did actually run Raman on the sample, but the results showed that the fiber was not made of fibrin, so he decided to not publish the results. And if McCairn did immunostaining with anti-fibrin antibodies, it would be an easy way to verify if the fibers that look like textile fibers are actually made of fibrin.
Did he even notice that UV radiation causes photochemical changes?
Case N, Johnston N, Nadeau J. Fluorescence Microscopy with Deep UV, Near UV, and Visible Excitation for In Situ Detection of Microorganisms. Astrobiology. 2024 Mar;24(3):300-317. doi: 10.1089/ast.2023.0020. PMID: 38507693; PMCID: PMC10979697.
Wong C, Pawlowski ME, Tkaczyk TS. Simple ultraviolet microscope using off-the-shelf components for point-of-care diagnostics. PLoS One. 2019 Apr 10;14(4):e0214090. doi: 10.1371/journal.pone.0214090. PMID: 30970020; PMCID: PMC6457486.
UV irradiation leads to the formation of a new fluorescence band in the 350–550 nm range, which corresponds to oxidation products of tyrosine residues. This effect has been observed for ubiquitin, human insulin, and Aβ(1–40)—that is, specifically for proteins lacking tryptophan residues:
Blue autofluorescence in protein aggregates “lighted on” by UV induced oxidation
“microinjecting 5–10 µl of ThT onto identified inclusions”
This inevitably results in:
local concentration peaks
diffusion gradients
osmotic pressure
fluid flows
recrystallization during drying
Did he adress?:
“The increase in fluorescence intensity above 5 µM ThT is likely to be due to micelle formation, which has been studied previously by Khurana et al. Khurana et al. show that ThT has a critical micelle concentration of approximately 4 µM, in good agreement with our observations that ThT becomes self-fluorescent at or above 5 µM. Formation of ThT micelles was also demonstrated by Sabaté et al. and Donnelly et al. To be clear, however, our results do not imply, nor are we suggesting, that ThT binds to amyloid in the form of micelles.
As shown in figure 2, when background ThT fluorescence is not corrected, higher Aβ40 concentrations at 2, 5 and 10 µM appear to have a different trend from the lower Aβ40 concentrations at 0.5 and 1 µM. Higher Aβ40 concentrations (2, 5 and 10 µM) show a bell-shaped profile with peak fluorescence at 20–50 µM ThT, while the lower Aβ40 concentrations (0.5 and 1 µM) show a continuous increase in fluorescence intensity over the entire range of ThT concentrations However, when background ThT signal is subtracted, all Aβ40 concentrations give similar bell-shaped profiles, with peak fluorescence at 20 µM ThT for Aβ40 fibril concentrations at 1–10 µM.”
Xue C, Lin TY, Chang D, Guo Z. Thioflavin T as an amyloid dye: fibril quantification, optimal concentration and effect on aggregation. R Soc Open Sci. 2017 Jan 4;4(1):160696. doi: 10.1098/rsos.160696. PMID: 28280572; PMCID: PMC5319338.
The fundamental methodological problem: no negative controls, no concentration data, no defined exposure parameters—and it ignores the fact that each step could independently produce the observed signal—without any amyloid
The fiber in the 4th image was already autofluorescent even without the ThT staining, so it's not clear to what extent the ThT enhanced the fluorescence of the fibers. He should've shown fluorescence micrographs of each fiber first without ThT and then with ThT. But he only showed one but not the other.
BTW McCairn screwed up the scale bars in the first 6 images, because they were actually about 200 µm and not 50 µm wide. So the fibers had a diameter around 10-20 µm, which is consistent with various textile fibers.
"The presence of intrinsic UV-reactive fibrillar microclots, in both stained and unstained slides, suggests a high degree of structural β-sheet order—indicative of amyloidogenesis."
Take three for the price of one!:
UV reactivity -> β-sheet structure: False. UV reactivity is a property of all aromatic amino acids, regardless of their secondary structure.
Stollar EJ, Smith DP. Uncovering protein structure. Essays Biochem. 2020 Oct 8;64(4):649-680. doi: 10.1042/EBC20190042. Erratum in: Essays Biochem. 2021 Jul 26;65(2):407. doi: 10.1042/EBC-2019-0042C_COR. PMID: 32975287; PMCID: PMC7545034
Moran SD, Zhang TO, Decatur SM, Zanni MT. Amyloid fiber formation in human γD-Crystallin induced by UV-B photodamage. Biochemistry. 2013 Sep 10;52(36):6169-81. doi: 10.1021/bi4008353. Epub 2013 Aug 29. PMID: 23957864; PMCID: PMC3859806.
Lucas LH, Ersoy BA, Kueltzo LA, Joshi SB, Brandau DT, Thyagarajapuram N, Peek LJ, Middaugh CR. Probing protein structure and dynamics by second-derivative ultraviolet absorption analysis of cation-{pi} interactions. Protein Sci. 2006 Oct;15(10):2228-43. doi: 10.1110/ps.062133706. Epub 2006 Sep 8. PMID: 16963649; PMCID: PMC2242397
Salmahaminati, Roca-Sanjuán D. The Photophysics and Photochemistry of Phenylalanine, Tyrosine, and Tryptophan: A CASSCF/CASPT2 Study. ACS Omega. 2024 Aug 6;9(33):35356-35363. doi: 10.1021/acsomega.4c00875. PMID: 39184496; PMCID: PMC11339992
Lucas LH, Ersoy BA, Kueltzo LA, Joshi SB, Brandau DT, Thyagarajapuram N, Peek LJ, Middaugh CR. Probing protein structure and dynamics by second-derivative ultraviolet absorption analysis of cation-{pi} interactions. Protein Sci. 2006 Oct;15(10):2228-43. doi: 10.1110/ps.062133706. Epub 2006 Sep 8. PMID: 16963649; PMCID: PMC2242397
Salmahaminati, Roca-Sanjuán D. The Photophysics and Photochemistry of Phenylalanine, Tyrosine, and Tryptophan: A CASSCF/CASPT2 Study. ACS Omega. 2024 Aug 6;9(33):35356-35363. doi: 10.1021/acsomega.4c00875. PMID: 39184496; PMCID: PMC11339992
β-sheet structure -> Amyloidogenesis: False. Normal proteins such as fibrin and immunoglobulins contain β-sheets without being amyloid.
Chiu ML, Goulet DR, Teplyakov A, Gilliland GL. Antibody Structure and Function: The Basis for Engineering Therapeutics. Antibodies (Basel). 2019 Dec 3;8(4):55. doi: 10.3390/antib8040055. PMID: 31816964; PMCID: PMC6963682
"Also, de novo designs of β proteins almost all have severe problems of insolubility and aggregation (3–6); many designs originally intended as globular β-sheet proteins have turned out instead to be valuable as models for amyloid-fiber formation."
Richardson JS, Richardson DC. Natural beta-sheet proteins use negative design to avoid edge-to-edge aggregation. Proc Natl Acad Sci U S A. 2002 Mar 5;99(5):2754-9. doi: 10.1073/pnas.052706099. PMID: 11880627; PMCID: PMC122420
Amyloidogenesis determined by light microscopy: Physically impossible. The β-sheet structure is defined by intermolecular distances of 0.47 nm. Means: far below the resolution of any light microscope.
Baxa U. Structural basis of infectious and non-infectious amyloids. Curr Alzheimer Res. 2008 Jun;5(3):308-18. doi: 10.2174/156720508784533367. PMID: 18537545; PMCID: PMC2570950
Cheng PN, Pham JD, Nowick JS. The supramolecular chemistry of β-sheets. J Am Chem Soc. 2013 Apr 17;135(15):5477-92. doi: 10.1021/ja3088407. Epub 2013 Apr 2. PMID: 23548073; PMCID: PMC3642101
Tycko R. Molecular Structure of Aggregated Amyloid-β: Insights from Solid-State Nuclear Magnetic Resonance. Cold Spring Harb Perspect Med. 2016 Aug 1;6(8):a024083. doi: 10.1101/cshperspect.a024083. PMID: 27481836; PMCID: PMC4968170
A year ago McCairn did an experiment where he mixed fibrinogen with ThT, heated it up to 42 degrees, and shook it, and as a result he claimed he was able to create string-shaped fibrin clots that were fluorescent with ThT staining. [https://rumble.com/v6uyxpb-lab-updates-synthesizing-amyloidogenic-fibrin.html?start=5979] He said: "In this instance using heat and shaking, we've managed to make the fibrinogen aggregate into an amyloidogenic form." [1:39:39]
He described one of the fibers as having a "twisted reactive profile that looks very similar to what we're seeing in the blood". [1:29:43] He was surprised to find fiber-like structures that looked similar to the so-called amyloid fibrin aggregates that he found in blood samples, even though his experiment was supposed to be a control run where he just looked at regular fibrinogen and he didn't apply any procedure to try to form amyloid fibrin, like mixing in LPS or spike protein peptides with the fibrin.
At time 1:18:12 he said "What I've done to try to remove confounders that - fibers, dust, et cetera that could get to our preparation - so every sample that we're using here, has been passed and filtered through a - basically anything larger than a 100 micrometers would not pass the filter". But he didn't mention that fibers from dust narrower than 100 µm might still pass through the filter. And a few minutes later he stated it as a fact that the fibers on his slide were amyloidogenic aggregates made of fibrin, and he didn't rule out the possibility that the fibers were just contaminants on his slide.
Two weeks ago when I asked McCairn why a fiber in a blood sample of one of his patients had a flat and not cylindrical cross-section, McCairn said it was because blood vessels are not cylindrical. [https://x.com/KevinMcCairnPhD/status/2045511293931819223] So he seemed to imply that the fiber was a clot that formed inside a blood vessel and then became dislodged, so that the clot conformed to the shape of the blood vessel. But at time 1:31:09 in the video from a year ago, you can see that one of the fibers on his slide had a similar flat shape, even though the fiber didn't form inside a blood vessel.
Let’s assume for a moment that McCairn actually found what he claims to have found: It is not possible to identify the main driver without taking into account the modRNA LNPs and the LNPs with minimal or no payload.
Pretorius and Kell have found a statistically significant difference in the level of amyloid microclots between subjects characterized as having long COVID and control subjects. [https://onlinelibrary.wiley.com/doi/10.1002/jmv.70613] The authors of the Nature paper from last month also found a significant elevation in amyloid microclots among subjects aged below 25 described as having long COVID. [https://www.nature.com/articles/s41390-026-05024-1But]
But I haven't seen any study of whether there would be a significant elevation in microclots among people characterized as vaccine injured, or among vaccinated people relative to unvaccinated people.
And even if there would be, the microclots wouldn't necessarily have anything to do with vaccines. Before COVID, Resia Pretorius found that the so-called amyloid microclots were associated with diabetes, Alzheimer's disease, Parkinson's disease, rheumatoid arthritis, psoriasis, lupus, and sepsis. [https://www.resiapretorius.net/research.html] For example in a study in 2017, her team found a significant elevation in microclots among subjects with diabetes relative to age-matched control subjects. [https://link.springer.com/article/10.1186/s12933-017-0624-5] In the pre-COVID studies, Pretorius's team attributed the amyloid microclots to LPS, and found that they could reduce the level of the clots by LPS-binding protein.
So the presence of the microclots might be a marker of overall poor health, and the association of the clots with long COVID might not even have anything to do with an interaction with the spike protein.
People like McCairn have connected the microclots to vaccines by equating the microclots with calamari clots, or by suggesting that the calamari clots are larger versions of the microclots, but I think the calamari clots are not real. People came up with the hypothesis that the calamari clots were made of amyloid fibrin in 2022, when the studies of Pretorius and Kell were already well-known. Competing hypotheses included that the calamari clots were made of hydrogel, that they were not made of protein but mostly metals, that they contained hydras, and that they were made of tissue that was programmed to grow snake venom glands by nanobots. But I guess the "amyloid fibrin" hypothesis ended up becoming more popular than the competing hypotheses, because it was more mundane so it was more believable.
In general the story about the clots has become more popular than other Stew ops like hydras and snake venom, because the clots are more mundane so they are more believable. Few people even realize that the existence of the calamari clots was first revealed to the world on the Jane Ruby Show, or that the film about the clots was a sequel to a film that said COVID was caused by snake venom in tap water.
Surely a simple route IMHO to demonstrate infectious amyloids (misfolded proteins etc). Would be to take what they had filtered from the patients and seed this into a control blood sample(s). If indeed infectious, there would be direct evidence where the control sample would multiply beyond any doubts? Then there would also be a large and sufficient sample to test, measure and properly identify?
I’m not qualified enough to interpret microscopic images in detail. But I can very quickly identify and understand what I need to know to assess whether a method is flawed or not and whether an argument is valid or not. And the whole “spike” theory consists of a series of assumptions and flawed experiments involving peptides or truly bizarre methods.
The real issue, which almost nobody took into account: The entire physicochemistry of LNPs was ignored because few people bothered to read all the literature on LNPs and failed to realize that they were injecting a colloidal, open system.
On the page of his website where McCairn advertises his "amyloid burden" detection service, there are two images of the same fiber that he found in Lyndsey's blood in 2024, where both images show the fiber after ThT staining but the other image is taken in UV mode. [https://synapteklabs.com/protocol-on-sending-blood-samples-2/] In the stream where McCairn showed the fiber, he only showed the sample after ThT staining, but he didn't show if the fiber was already autofluorescent before the staining, so the fluorescence may have not even been because of the ThT. [https://rumble.com/v5zq84w-operation-blue-drone-and-lessons-in-fluorescent-microscopy-amyloid-signals-.html?start=7301] Some other fibers McCairn has shown have already been autofluorescent before ThT staining, but McCairn seems to consider that to be sufficient evidence that the fibers are made of "amyloidogenic fibrin", even though for example textile fibers that have been bleached white can be strongly autofluorescent, like how white t-shirts are fluorescent under UV light.
In one stream McCairn even found some random autofluorescent fibers in a Moderna vaccine sample. [https://sars2.net/clot3.html, search for Moderna] At one point of the stream, he showed a fiber in non-UV mode and without ThT staining, and then when he applied ThT on the sample and switched to UV mode, he said that the fiber now glowed brighter than the background. However he failed to mention that a few minutes earlier when he had not yet applied the ThT, he panned past the fiber in UV mode, so you could see the fiber was already autofluorescent even without the ThT. Later he said "I can't explain the takeup of Thioflavins", but he didn't mention that the same fiber that supposedly took up Thioflavin was autofluorescent even without the ThT.
Last year when Nicolas Hulscher said that McCairn found "amyloid fibrils" in the 3-year-old's blood, Ian Musgrave replied: "That's a cellulose fibre, not amyloid." [https://x.com/KevinMcCairnPhD/status/1959430726237168121] Then McCairn said: "No it isn't. It's amyloidogenic fibrin." And Musgrave said: "No, it is not. It's just a cellulose fibre. I've EMed enough real amyloids and sighted enough cellulose fibres under the microscope to know which is which." And Musgrave said: "Thioflavin will stain almost anything if you don't use the right conditions, I have long experience with thioflavin and amyloids."
Then McCairn said: "No it doesn't when used at the right molar concentration, coupled with use of microinjection techniques to target the object. Besides cellulose doesn't auto-fluoresce. If you think it cellulose why don't recapitulate the slide with the fibrous clot being in-situ with the blood layer, and with connecting micro clot globular forms connecting each ends."
What he called the "globular forms" connected to the ends of the fiber were some random blobs on the slide that didn't even look connected to the fiber, and I don't think McCairn even verified if the blobs were made of fibrin or not. [https://sars2.net/clot3.html#Substack_post_about_SEM_images_of_the_3_year_olds_fiber] And McCairn forgot to mention that cellulose can be strongly fluorescent if it has been bleached white.
McCairn then replied that in order to eliminate false positives, "I run antibodies, use SEM/EDX, and Raman on samples". [https://x.com/KevinMcCairnPhD/status/1959414465293959358] I have told him to verify that his fibers are actually made of fibrin by doing either immunostaining with anti-fibrin antibodies or Raman spectroscopy, but I haven't seen him ever actually publish the results of either type of analysis (even though I don't know if by antibodies he meant anti-fibrin antibodies or antibodies to recognize amyloid proteins).
Last year McCairn published two Substack posts about the 3-year-old's fiber. In the first post he showed light microscope images of the sample, and he indicated that he was next going to run SEM, EDX, and Raman on the sample. [https://substack.com/@kevinwmccairnphd282302/p-164383206] In the second post he posted SEM images of the sample but he didn't describe EDX or Raman results. When I asked him why he didn't publish the EDX or Raman results, he responded to me by doing a stream where he showed the EDX results, but he said that he couldn't do Raman "because the sample was sent on a glass slide, and you need quartz slides for Raman". [https://x.com/KevinMcCairnPhD/status/1961314002304438763] But then I pointed out that McCairn had earlier said that the sample was preserved for Raman, and a glass slide may have been acceptable for Raman according to LLMs. And he already knew in advance that the sample was on a glass slide, so why did he even say he was going to do Raman?
I still suspect that he did actually run Raman on the sample, but the results showed that the fiber was not made of fibrin, so he decided to not publish the results. And if McCairn did immunostaining with anti-fibrin antibodies, it would be an easy way to verify if the fibers that look like textile fibers are actually made of fibrin.
“Methodology: Thioflavin T staining and autofluorescence imaging via UV light microscopy (4x, scale bar 50 µM scale); samples preserved for SEM/EDX”
https://substack.com/@kevinwmccairnphd282302/p-164383206
Did he even notice that UV radiation causes photochemical changes?
Case N, Johnston N, Nadeau J. Fluorescence Microscopy with Deep UV, Near UV, and Visible Excitation for In Situ Detection of Microorganisms. Astrobiology. 2024 Mar;24(3):300-317. doi: 10.1089/ast.2023.0020. PMID: 38507693; PMCID: PMC10979697.
Wong C, Pawlowski ME, Tkaczyk TS. Simple ultraviolet microscope using off-the-shelf components for point-of-care diagnostics. PLoS One. 2019 Apr 10;14(4):e0214090. doi: 10.1371/journal.pone.0214090. PMID: 30970020; PMCID: PMC6457486.
UV irradiation leads to the formation of a new fluorescence band in the 350–550 nm range, which corresponds to oxidation products of tyrosine residues. This effect has been observed for ubiquitin, human insulin, and Aβ(1–40)—that is, specifically for proteins lacking tryptophan residues:
Blue autofluorescence in protein aggregates “lighted on” by UV induced oxidation
https://www.sciencedirect.com/science/article/abs/pii/S157096391930144X
Then he writes:
“microinjecting 5–10 µl of ThT onto identified inclusions”
This inevitably results in:
local concentration peaks
diffusion gradients
osmotic pressure
fluid flows
recrystallization during drying
Did he adress?:
“The increase in fluorescence intensity above 5 µM ThT is likely to be due to micelle formation, which has been studied previously by Khurana et al. Khurana et al. show that ThT has a critical micelle concentration of approximately 4 µM, in good agreement with our observations that ThT becomes self-fluorescent at or above 5 µM. Formation of ThT micelles was also demonstrated by Sabaté et al. and Donnelly et al. To be clear, however, our results do not imply, nor are we suggesting, that ThT binds to amyloid in the form of micelles.
As shown in figure 2, when background ThT fluorescence is not corrected, higher Aβ40 concentrations at 2, 5 and 10 µM appear to have a different trend from the lower Aβ40 concentrations at 0.5 and 1 µM. Higher Aβ40 concentrations (2, 5 and 10 µM) show a bell-shaped profile with peak fluorescence at 20–50 µM ThT, while the lower Aβ40 concentrations (0.5 and 1 µM) show a continuous increase in fluorescence intensity over the entire range of ThT concentrations However, when background ThT signal is subtracted, all Aβ40 concentrations give similar bell-shaped profiles, with peak fluorescence at 20 µM ThT for Aβ40 fibril concentrations at 1–10 µM.”
Xue C, Lin TY, Chang D, Guo Z. Thioflavin T as an amyloid dye: fibril quantification, optimal concentration and effect on aggregation. R Soc Open Sci. 2017 Jan 4;4(1):160696. doi: 10.1098/rsos.160696. PMID: 28280572; PMCID: PMC5319338.
The fundamental methodological problem: no negative controls, no concentration data, no defined exposure parameters—and it ignores the fact that each step could independently produce the observed signal—without any amyloid
The fiber in the 4th image was already autofluorescent even without the ThT staining, so it's not clear to what extent the ThT enhanced the fluorescence of the fibers. He should've shown fluorescence micrographs of each fiber first without ThT and then with ThT. But he only showed one but not the other.
BTW McCairn screwed up the scale bars in the first 6 images, because they were actually about 200 µm and not 50 µm wide. So the fibers had a diameter around 10-20 µm, which is consistent with various textile fibers.
Best part ever:
"The presence of intrinsic UV-reactive fibrillar microclots, in both stained and unstained slides, suggests a high degree of structural β-sheet order—indicative of amyloidogenesis."
Take three for the price of one!:
UV reactivity -> β-sheet structure: False. UV reactivity is a property of all aromatic amino acids, regardless of their secondary structure.
Stollar EJ, Smith DP. Uncovering protein structure. Essays Biochem. 2020 Oct 8;64(4):649-680. doi: 10.1042/EBC20190042. Erratum in: Essays Biochem. 2021 Jul 26;65(2):407. doi: 10.1042/EBC-2019-0042C_COR. PMID: 32975287; PMCID: PMC7545034
Moran SD, Zhang TO, Decatur SM, Zanni MT. Amyloid fiber formation in human γD-Crystallin induced by UV-B photodamage. Biochemistry. 2013 Sep 10;52(36):6169-81. doi: 10.1021/bi4008353. Epub 2013 Aug 29. PMID: 23957864; PMCID: PMC3859806.
Lucas LH, Ersoy BA, Kueltzo LA, Joshi SB, Brandau DT, Thyagarajapuram N, Peek LJ, Middaugh CR. Probing protein structure and dynamics by second-derivative ultraviolet absorption analysis of cation-{pi} interactions. Protein Sci. 2006 Oct;15(10):2228-43. doi: 10.1110/ps.062133706. Epub 2006 Sep 8. PMID: 16963649; PMCID: PMC2242397
Salmahaminati, Roca-Sanjuán D. The Photophysics and Photochemistry of Phenylalanine, Tyrosine, and Tryptophan: A CASSCF/CASPT2 Study. ACS Omega. 2024 Aug 6;9(33):35356-35363. doi: 10.1021/acsomega.4c00875. PMID: 39184496; PMCID: PMC11339992
Lucas LH, Ersoy BA, Kueltzo LA, Joshi SB, Brandau DT, Thyagarajapuram N, Peek LJ, Middaugh CR. Probing protein structure and dynamics by second-derivative ultraviolet absorption analysis of cation-{pi} interactions. Protein Sci. 2006 Oct;15(10):2228-43. doi: 10.1110/ps.062133706. Epub 2006 Sep 8. PMID: 16963649; PMCID: PMC2242397
Salmahaminati, Roca-Sanjuán D. The Photophysics and Photochemistry of Phenylalanine, Tyrosine, and Tryptophan: A CASSCF/CASPT2 Study. ACS Omega. 2024 Aug 6;9(33):35356-35363. doi: 10.1021/acsomega.4c00875. PMID: 39184496; PMCID: PMC11339992
β-sheet structure -> Amyloidogenesis: False. Normal proteins such as fibrin and immunoglobulins contain β-sheets without being amyloid.
Chiu ML, Goulet DR, Teplyakov A, Gilliland GL. Antibody Structure and Function: The Basis for Engineering Therapeutics. Antibodies (Basel). 2019 Dec 3;8(4):55. doi: 10.3390/antib8040055. PMID: 31816964; PMCID: PMC6963682
"Also, de novo designs of β proteins almost all have severe problems of insolubility and aggregation (3–6); many designs originally intended as globular β-sheet proteins have turned out instead to be valuable as models for amyloid-fiber formation."
Richardson JS, Richardson DC. Natural beta-sheet proteins use negative design to avoid edge-to-edge aggregation. Proc Natl Acad Sci U S A. 2002 Mar 5;99(5):2754-9. doi: 10.1073/pnas.052706099. PMID: 11880627; PMCID: PMC122420
Amyloidogenesis determined by light microscopy: Physically impossible. The β-sheet structure is defined by intermolecular distances of 0.47 nm. Means: far below the resolution of any light microscope.
Baxa U. Structural basis of infectious and non-infectious amyloids. Curr Alzheimer Res. 2008 Jun;5(3):308-18. doi: 10.2174/156720508784533367. PMID: 18537545; PMCID: PMC2570950
Cheng PN, Pham JD, Nowick JS. The supramolecular chemistry of β-sheets. J Am Chem Soc. 2013 Apr 17;135(15):5477-92. doi: 10.1021/ja3088407. Epub 2013 Apr 2. PMID: 23548073; PMCID: PMC3642101
Tycko R. Molecular Structure of Aggregated Amyloid-β: Insights from Solid-State Nuclear Magnetic Resonance. Cold Spring Harb Perspect Med. 2016 Aug 1;6(8):a024083. doi: 10.1101/cshperspect.a024083. PMID: 27481836; PMCID: PMC4968170
A year ago McCairn did an experiment where he mixed fibrinogen with ThT, heated it up to 42 degrees, and shook it, and as a result he claimed he was able to create string-shaped fibrin clots that were fluorescent with ThT staining. [https://rumble.com/v6uyxpb-lab-updates-synthesizing-amyloidogenic-fibrin.html?start=5979] He said: "In this instance using heat and shaking, we've managed to make the fibrinogen aggregate into an amyloidogenic form." [1:39:39]
He described one of the fibers as having a "twisted reactive profile that looks very similar to what we're seeing in the blood". [1:29:43] He was surprised to find fiber-like structures that looked similar to the so-called amyloid fibrin aggregates that he found in blood samples, even though his experiment was supposed to be a control run where he just looked at regular fibrinogen and he didn't apply any procedure to try to form amyloid fibrin, like mixing in LPS or spike protein peptides with the fibrin.
At time 1:18:12 he said "What I've done to try to remove confounders that - fibers, dust, et cetera that could get to our preparation - so every sample that we're using here, has been passed and filtered through a - basically anything larger than a 100 micrometers would not pass the filter". But he didn't mention that fibers from dust narrower than 100 µm might still pass through the filter. And a few minutes later he stated it as a fact that the fibers on his slide were amyloidogenic aggregates made of fibrin, and he didn't rule out the possibility that the fibers were just contaminants on his slide.
Two weeks ago when I asked McCairn why a fiber in a blood sample of one of his patients had a flat and not cylindrical cross-section, McCairn said it was because blood vessels are not cylindrical. [https://x.com/KevinMcCairnPhD/status/2045511293931819223] So he seemed to imply that the fiber was a clot that formed inside a blood vessel and then became dislodged, so that the clot conformed to the shape of the blood vessel. But at time 1:31:09 in the video from a year ago, you can see that one of the fibers on his slide had a similar flat shape, even though the fiber didn't form inside a blood vessel.
Let’s assume for a moment that McCairn actually found what he claims to have found: It is not possible to identify the main driver without taking into account the modRNA LNPs and the LNPs with minimal or no payload.
Pretorius and Kell have found a statistically significant difference in the level of amyloid microclots between subjects characterized as having long COVID and control subjects. [https://onlinelibrary.wiley.com/doi/10.1002/jmv.70613] The authors of the Nature paper from last month also found a significant elevation in amyloid microclots among subjects aged below 25 described as having long COVID. [https://www.nature.com/articles/s41390-026-05024-1But]
But I haven't seen any study of whether there would be a significant elevation in microclots among people characterized as vaccine injured, or among vaccinated people relative to unvaccinated people.
And even if there would be, the microclots wouldn't necessarily have anything to do with vaccines. Before COVID, Resia Pretorius found that the so-called amyloid microclots were associated with diabetes, Alzheimer's disease, Parkinson's disease, rheumatoid arthritis, psoriasis, lupus, and sepsis. [https://www.resiapretorius.net/research.html] For example in a study in 2017, her team found a significant elevation in microclots among subjects with diabetes relative to age-matched control subjects. [https://link.springer.com/article/10.1186/s12933-017-0624-5] In the pre-COVID studies, Pretorius's team attributed the amyloid microclots to LPS, and found that they could reduce the level of the clots by LPS-binding protein.
So the presence of the microclots might be a marker of overall poor health, and the association of the clots with long COVID might not even have anything to do with an interaction with the spike protein.
People like McCairn have connected the microclots to vaccines by equating the microclots with calamari clots, or by suggesting that the calamari clots are larger versions of the microclots, but I think the calamari clots are not real. People came up with the hypothesis that the calamari clots were made of amyloid fibrin in 2022, when the studies of Pretorius and Kell were already well-known. Competing hypotheses included that the calamari clots were made of hydrogel, that they were not made of protein but mostly metals, that they contained hydras, and that they were made of tissue that was programmed to grow snake venom glands by nanobots. But I guess the "amyloid fibrin" hypothesis ended up becoming more popular than the competing hypotheses, because it was more mundane so it was more believable.
In general the story about the clots has become more popular than other Stew ops like hydras and snake venom, because the clots are more mundane so they are more believable. Few people even realize that the existence of the calamari clots was first revealed to the world on the Jane Ruby Show, or that the film about the clots was a sequel to a film that said COVID was caused by snake venom in tap water.
Surely a simple route IMHO to demonstrate infectious amyloids (misfolded proteins etc). Would be to take what they had filtered from the patients and seed this into a control blood sample(s). If indeed infectious, there would be direct evidence where the control sample would multiply beyond any doubts? Then there would also be a large and sufficient sample to test, measure and properly identify?
My thinking 🤔
I’m not qualified enough to interpret microscopic images in detail. But I can very quickly identify and understand what I need to know to assess whether a method is flawed or not and whether an argument is valid or not. And the whole “spike” theory consists of a series of assumptions and flawed experiments involving peptides or truly bizarre methods.
The real issue, which almost nobody took into account: The entire physicochemistry of LNPs was ignored because few people bothered to read all the literature on LNPs and failed to realize that they were injecting a colloidal, open system.
On the page of his website where McCairn advertises his "amyloid burden" detection service, there are two images of the same fiber that he found in Lyndsey's blood in 2024, where both images show the fiber after ThT staining but the other image is taken in UV mode. [https://synapteklabs.com/protocol-on-sending-blood-samples-2/] In the stream where McCairn showed the fiber, he only showed the sample after ThT staining, but he didn't show if the fiber was already autofluorescent before the staining, so the fluorescence may have not even been because of the ThT. [https://rumble.com/v5zq84w-operation-blue-drone-and-lessons-in-fluorescent-microscopy-amyloid-signals-.html?start=7301] Some other fibers McCairn has shown have already been autofluorescent before ThT staining, but McCairn seems to consider that to be sufficient evidence that the fibers are made of "amyloidogenic fibrin", even though for example textile fibers that have been bleached white can be strongly autofluorescent, like how white t-shirts are fluorescent under UV light.
In one stream McCairn even found some random autofluorescent fibers in a Moderna vaccine sample. [https://sars2.net/clot3.html, search for Moderna] At one point of the stream, he showed a fiber in non-UV mode and without ThT staining, and then when he applied ThT on the sample and switched to UV mode, he said that the fiber now glowed brighter than the background. However he failed to mention that a few minutes earlier when he had not yet applied the ThT, he panned past the fiber in UV mode, so you could see the fiber was already autofluorescent even without the ThT. Later he said "I can't explain the takeup of Thioflavins", but he didn't mention that the same fiber that supposedly took up Thioflavin was autofluorescent even without the ThT.