# Amyloid

Category: Conditions

Amyloid is the old term for the "starchy" appearing (including the way it stains) proteins seen in various diseases, and in the brain in Alzheimer's disease.

10 passages · 2 authors · 2006–2022 · Most-cited: [Ray Peat](https://bioenergeticoracle.com/md/voices/ray-peat/index.md)

Canonical page: https://bioenergeticoracle.com/concepts/amyloid

## Synthesis

**Amyloid** is a type of protein that forms fibrils and plaques through a structural rearrangement into a *beta pleated sheet* configuration, a process Peat identified as a common degenerative feature in practically all aged tissues and accelerated by radiation, toxins, and estrogen. [Source 3, 7] The formation of these fibrils begins when normal helical protein structures break down and roll over against themselves, creating sheets that stick to similar structures on other protein molecules, forming long fibrils that condense into the visible plaques characteristic of Alzheimer's disease and other amyloidoses. [Source 3] Peat traced the intellectual history of amyloid degeneration to E. J. Field's 1970s observations that aging tissues and virally-affected tissues showed similar inclusion bodies, and that scrapie-infected young tissues developed antigens identical to those in old tissues, work that anticipated the prion hypothesis but was omitted from official histories. [Source 1, 6]

The condensation of amyloid proteins is fundamentally linked to **carbon dioxide** and cellular energy status. Peat argued that carbon dioxide spontaneously combines with amino groups in proteins, stabilizing their normal functional conformation, and that the loss of carbon dioxide affects the structure of all proteins in the body. [Source 6] In the high-energy rested state, cell water behaves as if colder than its real temperature, allowing proper protein-folding, but a slight increase in water disorder can induce functional proteins to change conformation and spontaneously associate into fibrous masses. [Source 1, 6] The transthyretin protein, which carries thyroid hormone and vitamin A, resists condensation into amyloid fibrils when binding its normal ligands, but without them it can create toxic fibrils. [Source 1, 6] Glycation—the attachment of sugar molecules to proteins occurring when glucose consumption and carbon dioxide production fail—imitates mutated protein forms and creates preferred sites for prion-like protein deposition in the extracellular matrix. [Source 4]

**Polyunsaturated fatty acids** (PUFA) and their toxic breakdown products are central drivers of amyloid formation. Peat emphasized that the folding of proteins into amyloid fibrils is intensified by free fatty acids if they are polyunsaturated, and that chronic starvation or stress exposure releases these PUFA, creating a chain reaction effect that produces the neurofibrillary tangles and structural changes of the Alzheimer's brain. [Source 5] The prion protein produces its damage by activating lipases that release polyunsaturated fatty acids and produce lipid peroxides, while **acrolein**, a highly reactive product of PUFA degradation found at high levels in Alzheimer's brains, reacts with lysine in proteins and inhibits mitochondrial cytochrome oxidase, decreasing energy production. [Source 8] Serum amyloid A, which can increase 1000-fold under proinflammatory cytokines from irradiation, stress, trauma, or infection, activates phospholipase A2, releasing fatty acids and generating toxic aldehydes like 4-hydroxynonenal. [Source 2]

Estrogen plays a particularly damaging role in amyloid pathology. Peat noted that any tissue injury activates aromatase, the enzyme that creates estrogen, and that this happens in the Alzheimer's brain. [Source 5] Estrogen increases inflammation-associated substances including IL-6, C-reactive protein, and amyloid, liberates fatty acids, increases fibrinogen, and decreases albumin, increasing capillary leakiness. [Source 2] Serum amyloid P, called "the female protein" in hamsters due to its association with estrogen, can bind other amyloid proteins together and accelerate fibril formation. [Source 2] Estrogen also damages mitochondria in multiple ways, shifting metabolism away from glucose oxidation and impairing the enzyme that uses oxygen, while blocking the conversion of cholesterol into protective steroid hormones in the brain. [Source 5] Radiation imitates estrogen in its biological actions, and Peat stated that even low-energy inputs like ultrasounds or microwaves can produce amyloid fibrils in vitro. [Source 3, 7]

The protective factors against amyloid degeneration include thyroid hormone, progesterone, and carbon dioxide. Thyroid hormone protects against excess estrogen and supports the respiratory production of carbon dioxide, which through its reversible binding to protein amino groups alters electrical charge, folding, and water association. [Source 4, 9] Progesterone and pregnenolone have been called antifibromatic steroids, and saturated fats are protective against free radical damage and can reverse liver fibrosis. [Source 9] Georgi Dinkov has written that the seminal study supporting the beta-amyloid hypothesis of Alzheimer's disease was directly fabricated, and that virtually all research and clinical trials based on that hypothesis over two decades failed to produce any significant treatment advance, suggesting the amyloid hypothesis as pursued by the pharmaceutical industry rests on fraudulent foundations. [Source 10]

## People also ask

### How does carbon dioxide prevent amyloid formation?

Peat argued that carbon dioxide spontaneously binds to amino groups in proteins, stabilizing their normal folded shape, and that its loss allows proteins to misfold and aggregate into amyloid fibrils.

### What role do polyunsaturated fats play in amyloid diseases?

The entry describes how free polyunsaturated fatty acids intensify amyloid fibril formation, and their breakdown products like acrolein damage mitochondria and create a chain reaction that produces the tangles seen in Alzheimer's disease.

### Why did Peat consider estrogen harmful in Alzheimer's pathology?

Peat noted that estrogen increases inflammatory amyloid proteins, liberates fatty acids, damages mitochondrial energy production, and that tissue injury in the Alzheimer's brain activates aromatase to create more estrogen locally.

## Related concepts

- [Age Pigment (Lipofuscin)](https://bioenergeticoracle.com/md/concepts/age-pigment-lipofuscin/index.md)
- [Glycation](https://bioenergeticoracle.com/md/concepts/glycation/index.md)
- [Alzheimer's and Dementia](https://bioenergeticoracle.com/md/concepts/alzheimer-s-and-dementia/index.md)
- [Association-Induction Hypothesis (Gilbert Ling)](https://bioenergeticoracle.com/md/concepts/association-induction-hypothesis-gilbert-ling/index.md)
- [ATP (Adenosine Triphosphate)](https://bioenergeticoracle.com/md/concepts/atp-adenosine-triphosphate/index.md)
- [Cataracts](https://bioenergeticoracle.com/md/concepts/cataracts/index.md)

## Cited passages

Passage numbers match the `[Source N]` markers in the synthesis above.

### Source 1 — BSE - mad cow - scrapie, etc.: Stimulated amyloid degeneration and the toxic fats

Ray Peat · Article · 2007 · https://raypeat.com/articles/aging/madcow.shtml

> amyloid particles are formed by different proteins. The transthyretin protein which is binding small molecules resists condensation into the amyloid fibrils, but without its normal vitamin A and thyroid hormone, it can create toxic fibrils. (Raghu, et al., 2002.)
>
> Around 1970 I read E. J. Field’s suggestion that aging tissues and tissues affected by viral diseases showed some similar structures (“inclusion bodies”) under the electron microscope. In following up those observations, it turned out that old tissues appeared to develop antigens “identical with, or similar to,” scrapie-infected young tissues. The premature aging caused by removal of the thymus gland in newborn animals produced similar results.
>
> Field’s group and others (e.g., Alpers) were clearly showing that the scrapie infection involved proteins, but not viruses with nucleic acids. In one of Field’s last publications (1978), he even suggested that the infectious process might depend on a structural rearrangement of the host’s molecules, similar to the idea which is now known as the “prion hypothesis.” Field’s suggestion was an important advance in the theory of aging, and the evidence supporting it is now voluminous, but that work has been omitted from the official histories.
>
> Although phenomena of “imprinting” and non-genetic inheritance had been established earlier, the dogmatism of genetics led the scientific establishment to reject everything that challenged the primacy of DNA. When I mentioned to my professors (in 1971) the evidence that scrapie was transmitted without nucleic acid, I could see from their reactions that it would be a very long time before much progress would be made in understanding the degenerative brain diseases. When the exact structure of the “infectious” protein was later worked out, and the 1997 Nobel Prize awarded (to Stanley Prusiner), I was surprised that no one from Field’s group was included. (In 1976, a nobel prize had been awarded to D.C. Gajdusek, for his promotion of the idea of “slow viruses” in general, and particularly for arguing that scrapie, CJD and kuru were caused by slow viruses.)
>
> In reading Prusiner’s autobiographical statements, I was even more surprised to see that he claimed to have been puzzled to find out, around 1983, that the infectious agent was a protein.

### Source 2 — BSE - mad cow - scrapie, etc.: Stimulated amyloid degeneration and the toxic fats

Ray Peat · Article · 2007 · https://raypeat.com/articles/aging/madcow.shtml

> Radiation damage to the brain is most visible early in life, and in old age. In 1955, Alice Stewart showed that prenatal x-rays increase the incidence of brain cancer, leukemia, and other cancers. In 1967, a study in Japanese bomb survivors found that prenatal exposure to radiation had reduced their head size and brain size. In 1979, Sternglass and Bell showed extremely close correspondence between scores on the SAT and prenatal exposure to radiation.
>
> Serum amyloid A, which can increase 1000-fold under the influence of proinflammatory cytokines, resulting from irradiation, stress, trauma, or infection, is an activator of phospholipase A2 (PLA2), which releases fatty acids. Some of the neurodegenerative states, including amyloid-prion diseases, involve activated PLA2, as well as increases in the toxic breakdown products of the polyunsaturated fatty acids, such as 4-hydroxynonenal. The quantity of PUFA in the tissues strongly determines the susceptibility of the tissue to injury by radiation and other stresses. But a diet rich in PUFA will produce brain damage even without exceptional stressors, when there aren’t enough antioxidants, such as vitamin E and selenium, in the diet.
>
> Amyloidosis has traditionally been thought of as a condition involving deposits mainly in blood vessels, kidneys, joints and skin and in extracellular spaces in the brain, and the fact that the “amyloid” stained in a certain way led to the idea that it was a single protein. But as more proteins--currently about 20--were identified in amyloid deposits, it was gradually realized that the deposits can be identified inside cells of many different tissues, before the larger, very visible, extracellular deposits are formed.
>
> There is evidence of a steady increase in the death rate from amyloidosis. It kills women at a younger age than men, often at the age of 50 or 60.
>
> Serum amyloid P is called “the female protein” in hamsters, because of its association with estrogen; castrated (or estrogen treated) males also produce large amounts of it, and its excess is associated with the deposition of amyloid (Coe and Ross, 1985). It can bind other amyloid proteins together, accelerating the formation of fibrils, but this function is probably just a variation of a normal function in immunity, tissue repair, and development.

### Source 3 — Ionizing Radiation in Context 2 — Politics & Science, 2009

Ray Peat · Interview · 2009

> **Jon Barkhausen:** So it sounds like our culture was basically in love with modern technological gadgets.
>
> **Ray Peat:** Just the same as it is now. Some differences [exist], but the same principles [apply].
>
> **Jon Barkhausen:** I’m sure most doctors have heard this information from a source that they respected, and have cut out most of the excessive practices.
>
> **Ray Peat:** Well yah. But the people who sell the equipment create mythologies, saying all those that warn you that radiation will accelerate aging are just quacks. Now, 60 years later, some of the best researchers show that radiation causes the formation of amyloid [fibrils], the type of substance that is incriminated in Alzheimer's disease, degenerative lung, kidney and pancreatic disease, and so on.
>
> **Jon Barkhausen:** Amyloid is a plaque?
>
> **Ray Peat:** It's a type of protein that forms plaques. Normally, the very common structure of a protein is that there are helix structures, a spiral piece of a chain of protein. And with a certain disturbance, those spirals can break down and roll over against themselves and make a sheet arrangement called a '[beta] pleated sheet' . And those sheets can stick to [others] similar sheet structures [from] another protein. This array of pleated sheets sticking together in different protein molecules forms a long fibril. And then those fibrils are what actually forms the plaque. So first, you form the degraded protein, and then proteins form fibers, and the fibers condense into the visible plaques that they call amyloid.

### Source 4 — Energy Structure and Carbon Dioxide A Realistic View of the Organism

Ray Peat · Newsletter · 2013

> Cells related to inflammation can produce amyloid, as well as remove it. Glycation, the attachment of sugar molecules to proteins, can happen quickly, and can occur either with or without enzyme catalysis. The failure of glucose consumption and of carbon dioxide production in Alzheimer's disease predisposes to glycation.
>
> Glycation imitates mutated forms of proteins, for example normal transthyretin behaves like the prion protein, forming amyloid. Transthyretin, the protein that carries thyroid hormone and vitamin A, is normally taken up along with cholesterol under the influence of thyroid hormone. Abnormal cholesterol metabolism is one of the traits associated with Alzheimer's disease. In the absence of thyroid-supported respiration, carbon dioxide and other respiration-associated molecules (e.g., acetate) are replaced by lactate and unused sugar, causing abnormal modifications of proteins such as tau, which regulates microtubule assembly. Glycation of collagen in the extracellular matrix alters the properties of the matrix. The glycated matrix would become a preferred site for glycated prion-like proteins.
>
> It is possible that the altered transthyretin makes vitamin A less available to cells. Vitamin A deficiency creates major disruption of the framework proteins. Fragments of starch molecules inhibit the enzymes that remove inappropriately bound sugar molecules from proteins, and the inability to metabolize sugar into carbon dioxide increases that binding. Starches and unsaturated fats cooperate in this process of inappropriate sugar binding, while thyroid hormone, and the carbon dioxide it produces, tend to prevent the binding.
>
> Considering the universal importance of carbon dioxide to life, the ways it interacts with all of the important substances that make up organisms, that it is involved closely with ATP synthesis and other energy-related processes, that it participates intimately in the regulation of water and ions, that it is therapeutic in a range of conditions including angina pectoris, hypoxia, epilepsy, inflammation, shock, lipid peroxidation, pneumonia, and asthma, I think we can at least conclude that it is a largely overlooked mediator between chemical energy and life processes. In many cases, its movements and reactions constitute the actual motive force that so many fantasy theories have failed to explain. In other situations, it fills out the context for understanding the energy-mediating actions of ATP, calcium, and hormones.

### Source 5 — Ask the Herb Doctor: Dementia and Progesterone

Ray Peat · Interview · Dec 21, 2012 · http://l-i-g-h-t.com/files/herb-octors-dementia-and-progesterone-60-mins.mp4

> ## Alzheimer's, Amyloid, and Estrogen
>
> **Andrew Murray:** Would you explain why this energy failure is in part responsible for Alzheimer's?
>
> **Ray Peat:** The features that people consider to define Alzheimer's in the last 10 or 20 years have been the amyloid plaques and the neurofibrillary tangles. It happens that the folding of these proteins that form amyloid fibrils is intensified by free fatty acids if they're polyunsaturated.
>
> **Sarah Murray:** And those are released into the bloodstream when your liver runs out of sugar, basically, or you're starving.
>
> **Ray Peat:** Yeah. So chronic starvation, chronic exposure to polyunsaturated free fatty acids, or chronic exposure to stress is a major factor in creating the amyloid. The amyloid has a chain reaction effect, creating the tangles, the phosphorylation of Tau protein, and the whole structural change typical of the Alzheimer's brain. But any injury to any tissue, anywhere in the body, happens to activate the enzyme which creates estrogen. It's like when you injure a tree, it causes sprouting by turning on hormones in response to the injury. That's how estrogen works. Many enzymes get turned on, but especially aromatase, which is the basic former of estrogen itself. So in stress or any injury, aromatase appears and begins making estrogen right inside the tissue. And that happens in the Alzheimer's brain.

### Source 6 — BSE - mad cow - scrapie, etc.: Stimulated amyloid degeneration and the toxic fats

Ray Peat · Article · 2007 · https://raypeat.com/articles/aging/madcow.shtml

> # BSE - mad cow - scrapie, etc.: Stimulated amyloid degeneration and the toxic fats
>
> I have written before about the protective effects of carbon dioxide and progesterone, especially for the brain, and how the structure of cell water is affected by adsorbed and dissolved materials, and by metabolic energy. In the high energy (rested) state, cell water behaves as if it were colder than its real temperature, and this affects the behavior of proteins and fats in the cell, allowing “oily” surfaces to remain in contact with the more orderly water. Carbon dioxide spontaneously combines with the amino groups in proteins, stabilizing the normal functional conformation. The loss of carbon dioxide affects the structure of all proteins in the body, and the loss of cellular energy affects the structure of the intracellular proteins and their associated molecules.
>
> In scrapie and many other degenerative diseases (the amyloidoses), proteins condense into fibrils that tend to keep enlarging, with a variety of very harmful effects. The condensation of the “amyloid” proteins is sensitive to temperature, and a slight increase in the disorder of the water can induce functional proteins to change their conformation so that they spontaneously associate into fibrous masses. In the absence of sufficient carbon dioxide, all proteins are susceptible to structural alteration by the addition of sugars and fats and aldehydes, especially under conditions that favor lipid peroxidation.
>
> The amyloidoses affect different tissues in different ways, but when they occur in the brain, they produce progressive loss of function, with the type of protein forming the fibrils determining the nature of the functional loss. The protein which carries thyroid hormone and vitamin A, transthyretin, can produce nerve and brain amyloid disease, but it can also protect against other amyloid brain diseases; in Alzheimer’s disease, Parkinson’s disease, Huntington’s disease, and the “prion diseases” (scrapie, kuru, CJD, BSE, etc.) amyloid particles are formed by different proteins. The transthyretin protein which is binding small molecules resists condensation into the amyloid fibrils, but without its normal vitamin A and thyroid hormone, it can create toxic fibrils. (Raghu, et al., 2002.)

### Source 7 — Ionizing Radiation in Context 2 — Politics & Science, 2009

Ray Peat · Interview · 2009

> **Jon Barkhausen:** And that's a common symptom in all Alzheimer's patients?
>
> **Ray Peat:** Yes. And it's turning up in practically all aged tissues. But it's accelerated by radiation, toxins, estrogen, and even microwaves, and other types of disturbing energies. [For example,] in vitro , you could produce amyloid fibrils with energies as low as [the one emanating from] ultrasounds or microwaves.
>
> **Jon Barkhausen:** I thought ultrasound is actually protective of tissue. But, I guess, it does have some drawbacks then.
>
> **Ray Peat:** Yes. Everything that puts energy into cells and tissues in unbiological ways can cause some disruption.
>
> **Jon Barkhausen:** I can see how that would be. We were talking to Professor Gilbert Ling a few weeks ago. And he was basically talking about the electrical nature of living tissue, how everything is basically in an electrical relationship, all the proteins and the water within a cell.

### Source 8 — The Great Fish Oil Experiment

Ray Peat · Article · 2008 · https://raypeat.com/articles/articles/fishoil.shtml

> Apparently, anything that depletes the cell's energy, lowering ATP, allows an excess of calcium to enter cells, contributing to their death (Ray, et al., 1994).
>
> Increasing intracellular calcium activates phospholipases, releasing more polyunsaturated fats (Sweetman, et al., 1995)
>
> The acrolein which is released during lipid peroxidation inhibits mitochondrial function by poisoning the crucial respiratory enzyme, cytochrome oxidase, resulting in a decreased ability to produce energy (Picklo and Montine, 2001). (In the retina, the PUFA contribute to light-induced damage of the energy producing ability of the cells [King, 2004], by damaging the same crucial enzyme.)
>
> Besides inhibiting the ability of nerve cells to produce energy from the oxidation of glucose, acrolein inhibits the ability of cells to regulate the excitatory amino acid glutamate (Lovell, et al., 2000), contributing to the excitatory process.
>
> High levels of acrolein (and other products of PUFA degradation) are found in the brain in Alzheimer's disease (Lovell, et al., 2001).
>
> The "prion" diseases, CJD and TSE/BSE (mad cow disease) have many features in common with Alzheimer's disease, and several studies have shown that the "prion" protein produces its damage by activating the lipases that release polyunsaturated fatty acids and produce lipid peroxides (Bate, et al., 2004, Stewart, et al., 2001).
>
> Acrolein reacts with DNA, causing "genetic" damage, and also reacts with the lysine in proteins, for example contributing to the toxicity of oxidized low density lipoproteins (LDL), the proteins that carry cholesterol and that became famous because of their involvement in the development of atherosclerosis that was supposedly caused by eating saturated fats.
>
> My newsletter on mad cow disease discussed the evidence incriminating the use of fish meal in animal feed, as a cause of the degenerative brain diseases, and earlier newsletters (glycemia, and glycation) discussed the reasons for thinking that inappropriate glycation of lysine groups in proteins, as a result of a lack of protective carbon dioxide/carbamino groups, produces the amyloid (or "prion") proteins that characterize the dementias.

### Source 9 — Leakiness, aging, and cancer

Ray Peat · Article · 2006 · https://raypeat.com/articles/articles/leakiness.shtml

> (Veech and Gitomer, 1988, Veech and Fowler, 1987.) Dialysis has been seen to increase lung permeability Bell, et al., 1988).
>
> Amyloidosis produced by chronic dialysis affects all organs, but its effects are best known in the brain, heart, kidneys, and lungs. Serum amyloid-A is one of the acute phase proteins, like C-reactive protein (CRP), that are produced by inflammation. Estrogen, radiation and other stresses increase those pro-inflammatory acute phase proteins, and decrease protective albumin, which is called a "negative acute phase protein," since it decreases when the other acute phase proteins increase. The liver is the major source of the acute phase proteins, and it is constantly burdened by toxins absorbed from the bowel; disinfection of the bowel is known to accelerate recovery from stress.
>
> Seen from the perspective of the stress-leakage syndrome, any serious injury or sickness damages all organs.
>
> The exhaled breath is being used to diagnose inflammatory lung disease, since so many of the mediators of inflammation are volatile, but systemic diseases such as cancer and arthritis, and relatively minor stress can be detected by changes in the chemicals found in the breath. Polyunsaturated fats and their breakdown products--aldehydes, prostaglandins, isoprostanes, hydrocarbons, and free radicals--and carbon monoxide, nitric oxide, nitrite, and hydrogen peroxide are increased in the breath by most stresses.
>
> Both proline and glycine (which are major amino acids in gelatin) are very protective for the liver, increasing albumin, and stopping oxidative damage.
>
> Saturated fats are protective against free radical damage and can reverse liver fibrosis.
>
> Thyroid hormone protects against excess estrogen, and can prevent or reverse fibrosis of the heart.
>
> Antiestrogens are widely effective against vascular leakage. Thyroid, progesterone, and testosterone are among the most effective natural antiestrogens, and they are curative in many conditions that involve vascular leakage. Progesterone and pregnenolone have been called the antifibromatic steroids, and it has been used to treat many inflammatory and fibrotic diseases, including cancer.
>
> The antiserotonin drugs are being increasingly used to treat fibrotic diseases, and other problems related to vascular leakage.

### Source 10 — BREAKING: Seminal study, core of the amyloid-Alzheimer theory, was FABRICATED!

Georgi Dinkov · Article · Jul 22, 2022 · https://haidut.me/?p=1955

> It rarely gets any more damning for a scientific field than what was just announced today. Namely, the study considered the most important/influential in maintaining scientific support for the central dogma of dementia research – the beta-amyloid hypothesis of Alzheimer Disease (AD) – was not just wrong, but directly and deliberately FABRICATED in order to “better fit a hypothesis”. Here is the **cough** FRAUDULENT**cough**…I mean, “seminal”, study in question.
>
> [references]
>
> Now, against that news please consider also the article below, which states that virtually ALL research on AD over the last 2 decades failed to produce any significant advance in understanding or a treatment for that disease.
>
> [references]
>
> Since most of those clinical trials were based on the “amyloid hypothesis”, which we now know to be fraudulent, it is hard to see why the outcome of those trials would have been any different. In fact, the failure of all those trials is actually kind of amazing, as it suggests the trials themselves were/are still conducted with some form of scientific integrity. Otherwise, fabrications like the one described below would have occurred in at least one those trials considering the billions in costs for each one them and thus the incentive to cheat and get a drug (fraudulently) approved. Another amazing thing is that, as it has become usual, instead of doing a mea culpa and prosecuting the fraud to the fullest legal extent possible (given the massive poisoning effects the fraud had on science, as well as the direct harm to MILLIONS of innocent patients) the pharma industry and its medical supporters are trying to defend the amyloid link and continue to gaslight the public. I think that is probably the most depressing part of the article below – i.e. despite the obvious/open FRAUD it will still be “business as usual” – i.e. the industry will continue to both waste money on a fraudulent idea as well as harm innocent patients. So don’t expect true AD cures or even so-called disease-modifying therapies to come out of Big Pharma any time soon. Now, for many people who do not really follow pharma/medical news, it would probably be reasonable to just brush this aside as a serious but rare instance of scientific fraud that does not undermine the health system as a whole.

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