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Related Concept Videos

Amyloid Fibrils03:03

Amyloid Fibrils

Amyloid fibrils are aggregates of misfolded proteins.  Under most circumstances, misfolded proteins are either refolded by chaperone proteins or degraded by the proteasome. However, in the case of a mutation or a disease, these proteins can accumulate to form large clusters and often further assemble to form elongated fibers, called fibrils. 
Amyloid deposits were observed as early as 1639 in the liver and the spleen.   In 1854, Rudolph Virchow performed iodine staining, normally used to...
Amyloid Fibrils03:03

Amyloid Fibrils

Amyloid fibrils are aggregates of misfolded proteins.  Under most circumstances, misfolded proteins are either refolded by chaperone proteins or degraded by the proteasome. However, in the case of a mutation or a disease, these proteins can accumulate to form large clusters and often further assemble to form elongated fibers, called fibrils. 
Amyloid deposits were observed as early as 1639 in the liver and the spleen.   In 1854, Rudolph Virchow performed iodine staining, normally used to...
Alzheimer Disease ll: Pathophysiology01:23

Alzheimer Disease ll: Pathophysiology

Alzheimer disease involves structural changes in the brain that begin long before symptoms appear. The most distinctive features are extracellular neuritic plaques and intracellular neurofibrillary tangles.Neuritic plaques form in the cerebral cortex and around blood vessels. These plaques contain a dense core of beta-amyloid (Aβ)—a toxic protein fragment that clumps outside neurons. The core is surrounded by damaged neuronal extensions, as well as reactive astrocytes and microglia. Abnormal...
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Drugs affecting neurotransmitter synthesis can impact the adrenergic neuron and the synthesis of neurotransmitters. For example, α-methyltyrosine and carbidopa target specific enzymes involved in catecholamine synthesis. α-methyltyrosine inhibits the enzyme tyrosine hydroxylase, which converts tyrosine into dopamine. By blocking this enzyme, α-methyltyrosine reduces dopamine production and other catecholamines. Carbidopa, on the other hand, inhibits the enzyme dopa decarboxylase, which converts...
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Neurochemical Transmission: Sites of Drug Action

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Phenolic compounds prevent amyloid β-protein oligomerization and synaptic dysfunction by site-specific binding.

Kenjiro Ono1, Lei Li, Yusaku Takamura

  • 1Department of Neurology and Neurobiology and Aging, Kanazawa University Graduate School of Medical Science, Kanazawa 920-8640, Japan.

The Journal of Biological Chemistry
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Phenolic compounds like myricetin and rosmarinic acid prevent amyloid-beta (Aβ) aggregation and reduce toxicity in Alzheimer

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Preparation of Oligomeric β-amyloid1-42 and Induction of Synaptic Plasticity Impairment on Hippocampal Slices
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Neurodegeneration in an Animal Model of Chronic Amyloid-beta Oligomer Infusion Is Counteracted by Antibody Treatment Infused with Osmotic Pumps
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Published on: August 14, 2016

Area of Science:

  • Neuroscience
  • Biochemistry
  • Pharmacology

Background:

  • Alzheimer disease (AD) is characterized by amyloid-beta (Aβ) protein deposition in the brain.
  • Epidemiological studies suggest dietary phenolic compounds may reduce AD incidence.
  • Myricetin (Myr) and rosmarinic acid (RA) previously inhibited Aβ aggregation in vitro and in vivo.

Purpose of the Study:

  • To investigate the mechanistic basis of how phenolic compounds affect Aβ aggregation.
  • To analyze the impact of five phenolic compounds on Aβ oligomerization and synaptic toxicity.

Main Methods:

  • Assessed the effects of five phenolic compounds on the Aβ aggregation process.
  • Evaluated the impact of phenolic compounds on oligomer-induced synaptic toxicities.
  • Utilized Nuclear Magnetic Resonance (NMR) spectroscopy to analyze molecular interactions.

Main Results:

  • Phenolic compounds effectively blocked Aβ oligomerization.
  • Myricetin (Myr) induced significant NMR chemical shift changes in monomeric Aβ.
  • Both Myr and rosmarinic acid (RA) reduced cellular toxicity and synaptic dysfunction caused by Aβ oligomers.

Conclusions:

  • Myricetin and rosmarinic acid demonstrate potential in mitigating Alzheimer disease pathology.
  • These compounds may inhibit Aβ toxicity and early assembly through distinct binding mechanisms.
  • Further research into Myr and RA as therapeutic agents for AD is warranted.