Amyloid is a fibril protein with several additional molecules. Presently, 25 proteins have been reported as main fibril components. Many fibril proteins appear as fragments of larger precursors and for some types it is not clear whether fragmentation comes before or after fibrillation. The self-assembly by amyloid proteins can be speeded up by seeding with preformed fibrils. See Alzheimer's disease for information on natural ways to treat or prevent this condition. Beta-amyloid also causes nerve cell damage in the eye from blindness-inducing glaucoma.

Amyloid, diet and nutrition
It is my opinion that amyloid formation can be influenced by diet and the types of foods we eat. A healthy diet with many fresh vegetables and herbs - which contain many flavonoids - is less likely to lead to amyloid formation than a high sugar high trans fat diet. Eating cold water wish with lots of omega-3 fatty acids could also be helpful.

Natural Herbs and Amyloid Plaque prevention
Many herbal and dietary compounds and flavonoids probably block amyloid formation. Here are some examples and if you visit the articles there are links where you can purchase some of the products:

Acetyl l-carnitine is an antioxidant and brain enhancement nutrient.

Benfotiamine has been beneficial in a rodent study.
   Powerful beneficial effects of benfotiamine on cognitive impairment and beta-amyloid deposition in amyloid precursor protein/presenilin-1 transgenic mice.
   Brain. 2010 ; Department of Neurology, State Key Laboratory of Medical Neurobiology, Fudan University, Shanghai, China.
   Reduction of glucose metabolism in brain is one of the main features of Alzheimer's disease. Thiamine (vitamin B1)-dependent processes are critical in glucose metabolism and have been found to be impaired in brains from patients with Alzheimer's disease. However, thiamine treatment exerts little beneficial effect in these patients. Here, we tested the effect of benfotiamine, a thiamine derivative with better bioavailability than thiamine, on cognitive impairment and pathology alterations in a mouse model of Alzheimer's disease, the amyloid precursor protein/presenilin-1 transgenic mouse. We show that after a chronic 8 week treatment, benfotiamine dose-dependently enhanced the spatial memory of amyloid precursor protein/presenilin-1 mice in the Morris water maze test. Furthermore, it effectively reduced both amyloid plaque numbers and phosphorylated tau levels in cortical areas of the transgenic mice brains. Unexpectedly, these effects were not mimicked by another lipophilic thiamine derivative, fursultiamine, although both benfotiamine and fursultiamine were effective in increasing the levels of free thiamine in the brain. In the animal Alzheimer's disease model, benfotiamine appears to improve the cognitive function and reduce amyloid deposition via thiamine-independent mechanisms, which are likely to include the suppression of glycogen synthase kinase-3 activities.

Carnosine is a potent antixodiant and could be of benefit in reducing amyloid formation.

CoQ10, or coenzyme Q10, may be of benefit.

Curcumin, an extract from turmeric, may be helpful.

Fish oils, including EPA and DHA omega-3 fatty acids should be considered.

Hypericum perforatum, known as St. John's wort. In a microglial cell line pretreated with St. John's wort extract, the cell death evoked by treatment with amyloid-beta was attenuated significantly in a dose-dependent manner.

Myricetin inhibits beta-amyloid fibril formation, a key problem with Alzheimer's disease.

Uncaria rhynchophylla could be of benefit.

Amyloid disease
This disease is due to the deposition of amyloid in organs and tissues. Amyloid disease variants share common mechanisms which lead to protein fibril formation and deposition. Primary amyloidosis, while the most common form of amyloidosis, is a sporadic disease. Secondary (reactive) amyloidosis occurs in those with chronic inflammatory disease or cancer. Alzheimer disease, while very common in the aged population, is unpredictable except for those rare forms of familial Alzheimer disease with characterized mutations in specific genes.

Amyloid fibrils
The formation of amyloid fibrils is associated with various human medical disorders of unrelated origin. Recent research indicates that self-assembled amyloid fibrils are also involved in physiological processes in several micro-organisms. Yet, the molecular basis for the recognition and self-assembly processes mediating the formation of such structures from their soluble protein precursors is not fully understood. Short peptide models have provided novel insight into the mechanistic issues of amyloid formation, revealing that very short peptides (as short as a tetrapeptide) contain all the necessary molecular information for forming typical amyloid fibrils. A careful analysis of short peptides has not only facilitated the identification of molecular recognition modules that promote the interaction and self-assembly of fibrils but also revealed that aromatic interactions are important in many cases of amyloid formation. The realization of the role of aromatic moieties in fibril formation is currently being used to develop novel inhibitors that can serve as therapeutic agents to treat amyloid-associated disorders.

Beta amyloid protein
The principal component of amyloid is the beta-amyloid protein (A beta), a 39-43 amino acid peptide composed of a portion of the transmembrane domain and the extracellular domain of the amyloid precursor protein.

Amyloid eprodisate treatment
Treatment with eprodisate can slow the decline in renal function that usually occurs with amyloid A (AA) amyloidosis involving the kidneys. Eprodisate belongs to a new class of drugs that blocks amyloid build-up in various tissues by inhibiting the interactions of amyloidogenic proteins and glycosaminoglycans. The Eprodisate for amyloid A Amyloidosis Trial (EFAAT) involved 183 patients who were randomized to receive eprodisate or placebo for 24 months. The main outcome measure was disease worsening, defined as a doubling of serum creatinine levels, a fall in creatinine clearance by 50% or more, progression to end-stage kidney disease, or death. At 24 months, disease worsening was noted in 40% of control patients compared with 27% of those given eprodisate. Treatment with eprodisate was generally well tolerated with no increase in adverse events relative to placebo. Eprodisate works by directly targeting AA amyloid formation. EFAAT was funded, in part, by drugmaker Neurochem, which is planning to market eprodisate as Kiacta. N Engl J Med 2007.
   Comments: Would certain natural supplements work better? Too bad the research funding is not there for us to find out.