top of page
Amyloids & Prions
By Dr. Michael W. Roth

This paper will describe two inextricably connected entities, how they affect health, and treatment to remove: Amyloids and Prions.

Amyloids & Prions

A disturbing paper was published on June 13th, 2022 entitled: Neurotoxic amyloidogenic peptides in the proteome of SARS-COV2: potential implications for neurological symptoms in COVID-19”.

COVID-19 is primarily known as a respiratory disease caused by SARS-CoV-2. However, neurological symptoms such as memory loss, sensory confusion, severe headaches, and even stroke are reported in up to 30% of cases and can persist even after the infection is over (labeled “Long COVID”). These neurological symptoms are thought to be produced by the virus infecting the central nervous system; however the molecular mechanism triggering them is not fully understood. The neurological effects of COVID-19 share similarities to neurodegenerative diseases in which the presence of cytotoxic aggregated (clumping together) amyloid protein or peptides is a common feature.

Amyloids are tube-like proteins that are very small, about 7-13 nanometers in diameter (1 cm = 10,000,000 nm) and are linked to diseases such as Alzheimer’s which is known to be associated with amyloid protein accumulation.


Amyloid buildup is also found in COVID-19 Acute Respiratory Distress Syndrome (ARDS) where mechanical ventilation is often used for life support as oxygen levels drop, and in patients where it can trigger the formation of blood clots. These clots are resistant to typical blood thinners and prevent adequate oxygen supply, thus contributing to cell death and organ failure.


Interestingly, the spike protein of the SARS-CoV-2 can cause amyloid-forming proteins like Aß (beta-amyloid), along with a-synuclein, tau, prion, and d TAR DNA binding protein-43 (TDP-43) accumulation in the brain and explain the neurodegeneration seen in COVID-19 patients. This accumulation of amyloid blood clotting is also referred to as amyloidosis.

Following the hypothesis that some neurological symptoms of COVID-19 may also follow an amyloid etiology, two amyloidogenic peptides from the SARS-CoV-2 proteome that self-assemble into amyloid assemblies and are unique to SARS-nCoV-2 have been found. Furthermore, these amyloids form self-assembling crystalline structures independently and together at room temperature. They were shown to be highly toxic to neuronal cells causing programmed cell death (apoptosis) even at very low concentration.   

Summary: Two peptides of SARS-nCoV-2 induce apoptosis in human neural cells subsequently this is causing all neurological problems associated with COVID-19. Furthermore, the cytotoxicity and protease-resistant structure of these assemblies may result in their persistent presence in the CNS of patients post-infection that could partially explain the lasting neurological symptoms of COVID-19.

Question: If the modified spike protein in the COVID-19 injectable products contain amyloidogenic peptides capable of assembling into amyloid structures, is this why we are seeing such systemic neurological, hepatological, cardiovascular and reproductive damages with regard to adverse event reports in databases such as VAERS, Eudra and Yellowcard?


A study of interest is from Linköping University in Sweden entitled, Amyloidogenesis of SARS-CoV-2 Spike Protein.


The authors Sofie Nyström and Per Hammarström were able to separate several amyloids from the spike protein of the SARS-CoV-2 virus.


All proteins are made of 20 amino acids. The spike protein has 1,273 amino acids, which means the long spike protein can be cut into shorter proteins, typically broken down into smaller pieces by a protease enzyme (elastaste) made by neutrophils (the most abundant while blood cell and first line of defense against infections in the human body). Its purpose is to break down the proteins of invading germs.


However, in the presence of the spike protein the smaller proteins happen to readily misfold into prions (responsible for Mad Cow Disease and Creutzfeldt-Jakob disease (vCJD) in humans) producing amyloids (a conglomeration of many misshapen proteins aggregating together), which then accumulate to cause fibrils (long strings of fibrous-like material) that can branch out in multiple directions and grow in size in the bloodstream until either filling the vessels in which they ultimately lodge or else flow along like seeds for future proliferation into more and larger amyloid fibrils. These amyloid fibrils interact with constituents in the blood such as fibrin (and fibrinogen) that further enhance blood clotting and congealing. However, this fibrin strangely does NOT respond to plasmin which would typically eventually help break down the clots such that these clots full of amyloid fibrils, fibrin, fibrinogen, AND neutrophils and eosinophils (as previously reported by pathologist Dr. Ryan Cole after he examined such large and bizarre clots obtained from corpses during embalming procedures) are self-perpetuating.  

Variant Creutzfeldt–Jakob disease (vCJD) is one of the prion diseases in humans. It is highly associated with human intake of the bovine serum encephalopathy (BSE) pathogen. Therefore, foreign PrP fibrils possess cytotoxicity.

Clearly, this finding seems to explain in part or whole the instigating factors responsible for the incredible clots of blood with long and strong tails of whitish yellow material harvested from large vessels and reported on by embalmers. 

This could also be a major source of the historical rise in clotting disorders leading to sudden onset of disease and death being witnessed around the world where COVID injections have been administered in large numbers. 


The figure below shows the amyloid fibrils formed from a spike protein.


The Pfizer shot introduces spike protein mRNA, which forms spike proteins in the muscles. The neutrophils break down the spike proteins with neutrophil elastase and release amyloids as a response to the spike protein. The spike proteins also elicit a hyper immune response also known as a cytokine storm.

These cytotoxic amyloid aggregates of SARS-SoV-2 s are highly toxic to neuronal cells  which may trigger neurological symptoms in COVID-19.

How to get rid of amyloid?

There are no medicines to get rid of amyloid in the body—however, one author suggested intermittent fasting and adequate sleep to remove and wash the amyloid proteins away! A ridiculous suggestion – if only it were that easy. We will discuss a viable and much more realistic method at the conclusion.

A recent article discusses blood clots in the deceased

Postmortum studies of blood clots extracted from those who “suddenly died” have been found to routinely contain abnormal crystalline and fibrous structures, nanowires & chalky particles when viewed under a microscope. This takes place usually in a number of months following COVID vaccinations.

They are unusual in that they consist of more than mere blood cells. Normal clots are gelatinous; however those being found contain extremely large, complex, repeating structural elements appearing to be “constructed” in the blood of the victims who died from these clots.

All of reported clots were extracted from the blood vessels of patients within a few hours of their death and are not the result of post-mortem blood stasis or congealed blood. They were provided by reputable, active embalmer Richard Hirschman.


Below is a vial of these raw clots, washed of blood and preserved, before staining:

These structures exhibit the following unusual properties:

  • They are tough, fibrous and resilient, with properties similar to small rubber bands.

  • They consist of many small, fibrous strands exhibiting repeating patterns of scale-like engineering and silicon or microchip-like structure.

  • They contain unusual crystalline-like structures, exhibiting transparency and resistance to normal gram staining techniques and were prepared using different methodology.


Microscopy photo set #1: Crystal-like nanostructures

Here we see unusual crystalline structures that resist staining techniques and appear to show a kind of nano-scale, clear structure never seen in normal blood or clots.


Microscopy photo set #2: Structures, strands and particles

This set shows close-up details on the strands, structures and particles found in the blood clots.





Microscopy photo set #3: Crystal-shaped structures

Crystal-like structures are attached to the bark-like structure of the blood clot.



Microscopy photo set #4: Fibrous material is not simply congealed blood cells



Microscopy photo set #5: Silicon-like “chip” structure

This series shows what appears to resemble silicon-based microchip structures.


Microscopy photo set#6: Chalk-like white particles

An embalmer mentioned that blood emptied from the bodies of these people during embalming often appears to show “chalk-like” white particles which are visible even to the naked eye in certain cases.


Microscopy photo set#7: “Nanowire” structures and repeating, structural scales (not a human hair)

This, at first, appears to be a micro-scale wire. Magnification reveals a series of repeating structures along the top that appear to be nano-scale wire interface junctions.


At a magnification of 1500x blood cells would be clearly seen. However, they are missing in these structures. Rather they are proteins unnaturally constructed in the body’s cells by ribosomes altered by mRNA (COVID) gene therapy injections, which overwrite new instructions to the cells.

A serious concern is that these are programmed for time release with amyloid mRNA instructions to construct these fibrous structures, and could eventually block major arteries or cause heart attacks, strokes or other acute causes of “Sudden Adult Death Syndrome” (SADS).

Autophagy Modulation is being looked at as a Treatment of Amyloid Diseases

We’ve seen that amyloid diseases result from protein aggregation but also as the result of impaired amyloid clearance.

Typically, protein homeostasis, or proteostasis, is maintained by multiple cellular pathways—including protein synthesis, quality control, and clearance—which are collectively responsible for preventing protein misfolding or aggregation.

Modulating protein degradation is a very complex but attractive treatment strategy used to remove amyloid and improve cell survival.  Autophagy is an important clearance pathway of amyloid proteins, and strategies for using it as a potential therapeutic target for amyloid diseases.

Autophagy is a part of the wider lysosomal system [23]. This pathway is a crucial degradation pathway for unwanted or damaged organelles and proteins [24]. Dysfunction of the autophagy-lysosomal system has been implicated in the pathogenesis of many neurodegenerative diseases that feature increased accumulation of amyloid protein deposits. At the same time, stimulating this pathway to clear the toxic amyloid proteins has gained interest as a therapeutic strategy [25].

And, although autophagy activation is a promising intervention, there are some caveats to consider. While “rapamycin” is a potent medicinal autophagy activator, it has immunosuppressive effects as well as other pleiotropic effects resulting from the inhibition of mTOR, which also controls important cell processes including translation, cell growth and metabolism [77]. In cell models with impaired lysosomal clearance, inducing autophagy has shown to accelerate pathology, suggesting that the success of any autophagy-based intervention may depend on whether lysosomal clearance is functional.

One major drawback is the translatability of AD drugs from animal models to human clinical trials [85]. Additionally, AD pathology in humans develops over decades, while in transgenic mice the disease develops in just a few months and only with familial AD mutations [85]. Additionally, effects of autophagy activation may vary significantly depending on the physiological state of the cell—especially during proteotoxic stress. With regards to testing autophagy modulators in animal models, there is no congruent evidence to demonstrate that autophagy activation can provide benefits in late-stage disease with pre-existing pathology. In fact, some studies suggest that autophagy activation may be harmful in ageing conditions with pre-existing pathology [86].

Programmed cell death or apoptosis shares a number of biochemical pathways with autophagy and together they regulate stress response and cell survival [87].

In 2008, Carloni et al. showed that activation of autophagic pathways is a possible protective mechanism in the early stage of the brain ischemia.

Autophagy shows tumor suppressive qualities as well, as dysfunctional autophagy has been implicated in tumor development.

As we have seen, although autophagy shows potential in ameliorating amyloid congregations, there are still many drawbacks and not enough anecdotal or clinical evidence to use it as a viable treatment at the present time.


23. Boland B., Kumar A., Lee S., Platt F.M., Wegiel J., Yu W.H., Nixon R.A. Autophagy induction and autophagosome clearance in neurons: Relationship to autophagic pathology in Alzheimer’s disease. J. Neurosci. Off. J. Soc. Neurosci. 2008;28:6926–6937. doi: 10.1523/JNEUROSCI.0800-08.2008. [PMC free article] [PubMed] [CrossRef] [Google Scholar]

24. Dunn W.A., Jr. Autophagy and related mechanisms of lysosome-mediated protein degradation. Trends Cell Biol. 1994;4:139–143. doi: 10.1016/0962-8924(94)90069-8. [PubMed] [CrossRef] [Google Scholar]

25. Boland B., Yu W.H., Corti O., Mollereau B., Henriques A., Bezard E., Pastores G.M., Rubinsztein D.C., Nixon R.A., Duchen M.R., et al. Promoting the clearance of neurotoxic proteins in neurodegenerative disorders of ageing. Nat. Rev. Drug Discov. 2018 doi: 10.1038/nrd.2018.109. in press. [PMC free article] [PubMed] [CrossRef] [Google Scholar]

77. Sarkar S. Regulation of autophagy by mTOR-dependent and mTOR-independent pathways: Autophagy dysfunction in neurodegenerative diseases and therapeutic application of autophagy enhancers. Biochem. Soc. Trans. 2013;41:1103–1130. doi: 10.1042/BST20130134. [PubMed] [CrossRef] [Google Scholar]

85. Bharadwaj P. Animal Models of Alzheimer’s Disease. In: Martins R.N., Brennan C.S., Fernando W.B., Brennan M.A., Fuller S.J., editors. Neurodegeneration and Alzheimer’s Disease. John Wiley & Sons; Hoboken, NJ, USA: 2019. pp. 291–310. [Google Scholar]

86. Carosi J.M., Sargeant T.J. Rapamycin and Alzheimer disease: A double-edged sword? Autophagy. 2019;15:1460–1462. doi: 10.1080/15548627.2019.1615823. [PMC free article] [PubMed] [CrossRef] [Google Scholar]

87. Marino G., Niso-Santano M., Baehrecke E.H., Kroemer G. Self-consumption: The interplay of autophagy and apoptosis. Nat. Rev. Mol. Cell Biol. 2014;15:81–94. doi: 10.1038/nrm3735. [PMC free article] [PubMed] [CrossRef] [Google Scholar]



The above information in which prions were also mentioned is worthy of further discussion since prions and amyloid structures are connected.  

What are Prions?

Prions are found all over the body but the ones that cause diseases are structurally different. Few of them are even resistant to proteases. The two isoforms of prions are:

PrPc - These prion proteins are found on the cell membrane and play an important role in cell signaling and cell adhesion. More research is being carried out to discover its functions.

PrPsc - This is the disease-causing prion and is resistant to proteases. It affects the confirmation of PrPc and changes it. It also forms highly structured amyloid fibers. The other free proteins also attach to the end of these fibers. Similar prions with similar amino acids can only bind.  

Transmissible spongiform encephalopathies (TSEs) are fatal neurodegenerative diseases caused by misfolding and aggregation of prion protein (PrP).

Diseases Caused by Prions

Prions are quite rare and difficult to transmit. But they are progressive neurodegenerative diseases with no cure or treatment.

Prions can spread in a person’s brain for years without any symptoms. The prions start killing neurons and the symptoms strike the brain quickly causing the victim’s health to decline.

All the prion diseases are fatal, some last a few months, and some might last for years. A few experimental pieces of evidence show that the prions are not ordinary infectious materials. It is believed to be a “self-replicating protein” without any mechanical assistance. When a prion comes into contact with a normal protein, it makes the normal protein alter its shape, and become a prion also.

Types of Prion Diseases

Prion diseases can be of three types:

1. Acquired: this occurs when a person is exposed to the infectious protein. It is rare.
2. Genetic: this occurs as the result of genetic transmissions, yet not necessarily inherited from family. It may be caused due to the mutation in some DNA.
3. Sporadic: the exact cause is unknown and is the most common to date.

Symptoms of Prion diseases:

  • Developing dementia

  • Hallucinations

  • Fatigue

  • Stiffening of muscles

  • Confusion

  • Difficulty in speaking


Do COVID “Vaccines” Cause Prion Disease?

Steve Kirsch of the COVID-19 Early Treatment Fund apparently has proven that the COVID-19 injections are causing people to develop prion disease.

Before the shots were first introduced as part of Operation Warp Speed, prion disease was extremely rare. However, it is alarmingly pervasive since the vaccine rollout. 

Back in May 2021, Prof. Byram Bridle made public a FOIA (Freedom of Information Act) request about the Pfizer jab’s bio-distribution data. In this disclosure, it was mentioned that the spike protein was associated with Lewy body formation, which is linked to prion diseases such as dementia, Alzheimer’s, and Creutzfeldt-Jakob disease (CJD).

A VAERS (Vaccine Adverse Event Reporting System) query shows that the only injections causing seriously elevated rates of prion disease are those being administered for the COVID “virus”.  In fact, nearly 84 percent of all excess dementia and Alzheimer’s cases this past year are linked to Chinese Flu shots. For Creutzfeldt-Jakob disease, which is much rarer, that figure is nearly 86 percent.

Vaccines and prion disease

That vaccines might become contaminated with prions is not new. In fact, decades ago, during the height of the mad cow disease outbreak in the UK, there was indeed concern about using Fetal Bovine Serum from British herds of cattle to manufacture vaccines. A news article in Nature from 2000 reported on the findings of an inquiry into Britain’s BSE epidemic and even specifically asked the question: “Were some CJD victims infected by vaccines?

Alarmingly, vaccines produced after the point at which the BSE epidemic had been identified — possibly using British bovine material — were still in use as recently as November 1993. According to the inquiry’s report, the chief medical officer of the day, Donald Acheson, decided to phase out the existing stocks because new batches of vaccines take time to grow, and medical experts considered that the benefit of maintaining a continuous national immunization program outweighed the risk of interrupting it. Amazing!

A Treatment on the Horizon?

There is currently at least one study with computer simulations that has shown that polythiophenes could indeed fit into a space found on one end of a prion, and block it from connecting with normal proteins. Polythiophenes (PTs) are polymerized thiophenes, a sulfur heterocycle.

However, this may not be a viable solution. It remains to seen whether polythiophenes could be given safely to people — their toxicity is not yet known, and even further away are tests studying whether they may be effective in helping people with CJD.

What about Quercetin?

Quercetin, an antioxidant and flavonoid (a group of polyphenols) found naturally in several plant foods, in apples, onions, green tea, wine, and so on, has been promoted heavily as a treatment for COVID-19.  A recently published article in Pubmed now suggests that Quercetin Disaggregates Prion Fibrils and Decreases Fibril-Induced Cytotoxicity and Oxidative Stress.

According to the article, previous studies have demonstrated that quercetin can disaggregate some amyloid fibrils, such as amyloid β peptide (Aβ) and α-synuclein. However, the disaggregating ability is unclear in PrP fibrils (those known to cause disease in humans). The study was on mouse prion protein (moPrP). The results showed that quercetin treatment can disaggregate moPrP fibrils and lead to the formation of the proteinase-sensitive amorphous aggregates. Furthermore, quercetin-bound fibrils can reduce the membrane disruption of erythrocytes. Consequently, quercetin-bound fibrils cause less oxidative stress, and are less cytotoxic to neuroblastoma cells. The role of quercetin is distinct from the typical function of antiamyloidogenic drugs that inhibit the formation of amyloid fibrils.

Conclusion & Opinion

Quercetin has the same effect and the same role as many antioxidants. While helpful with normal immunity, COVID is a pathology far beyond what normal foods and supplements can effectively handle. They are absolutely essential for robust health and immunity, but when dealing with a super-virus or super-pathology, something more is needed. 

Dr. Roth: According to Dr. Garry Gordon considered the father of modern detox, EDTA may be the most powerful and effective antioxidant available due to its ability to tie up heavy metals and remove toxins. 

A first line in breaking down and reversing the amyloid/fibrin spike structure would be using an enzyme such as nattokinase and/or serrapeptase, but again, we have seen in previous articles that EDTA can safely and effectively breakdown and disintegrate biofilms, clots, and calcific deposits that have naturally and unnaturally accumulated in the body.

Dr. Michael Roth is a retired doctor of chiropractic with extensive knowledge and experience in nutrition and health. After running a successful chiropractic office for nearly 15 years, Dr. Roth branched out into peripheral realms of health study to enable him to offer his clients a more complete and overall knowledge base of wellness. With a goal to glorify the Lord, he is dedicated to provide for and educate the public regarding the gaining and maintaining of dynamic health and effective body cleansing. Dr. Roth also developed a unique topical EDTA cream for the safe, gentle and effective removal of toxic chemicals, graphene oxide, heavy metals and more from the body. 


bottom of page