Amyloid

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. 2 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. 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. 2

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. 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. 2 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. 2 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. 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. 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. 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. 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. 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. 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. 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. 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. 2

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. 2 Progesterone and pregnenolone have been called antifibromatic steroids, and saturated fats are protective against free radical damage and can reverse liver fibrosis. 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. 10