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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...
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Indirect-Acting Cholinergic Agonists: Chemistry and Structure-Activity Relationship

Indirect-acting cholinergic agonists are agents that interact with the acetylcholinesterase enzyme in the synaptic cleft, preventing the breakdown of acetylcholine into choline and acetate. Consequently, the concentration of acetylcholine in the synaptic cleft increases. These agonists can be classified into reversible and irreversible inhibitors based on their duration of action.
Reversible inhibitors display short to medium durations of action. Short-acting agents include simple alcohols with...

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Selection of Aptamers for Amyloid &beta;-Protein, the Causative Agent of Alzheimer&#39;s Disease
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Amyloid-binding compounds and their anti-prion potency.

Kenta Teruya1, Katsumi Doh-ura

  • 1Department of Neurochemistry, Tohoku University Graduate School of Medicine, Seiryo-cho, Aoba-ku, Sendai, 980-8575, Japan. doh-ura@med.tohoku.ac.jp.

Current Topics in Medicinal Chemistry
|September 25, 2013
PubMed
Summary

New amyloid-binding compounds show promise for diagnosing and treating prion diseases, like Gerstmann-Sträussler-Scheinker syndrome. However, their effectiveness varies across different prion strains and diseases lacking amyloid plaques, necessitating further research.

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Area of Science:

  • Neuroscience
  • Biochemistry
  • Pharmacology

Background:

  • Prion diseases, or transmissible spongiform encephalopathies, involve abnormal prion protein accumulation in the brain, sometimes forming amyloid plaques.
  • Amyloid-binding compounds are being investigated for their potential in diagnosing and treating these neurodegenerative conditions.

Purpose of the Study:

  • To review the utility of amyloid-binding compounds for the diagnosis and therapy of prion diseases.
  • To highlight novel styrylbenzoazole and phenylhydrazine derivatives with potential medicinal applications.

Main Methods:

  • Review of existing literature on amyloid-binding compounds and their application to prion diseases.
  • Case examples of specific compounds like BF-227 and compB in prion disease contexts.

Main Results:

  • Styrylbenzoazole derivative BF-227 shows diagnostic utility for Gerstmann-Sträussler-Scheinker syndrome.
  • Phenylhydrazine derivative compB demonstrates prophylactic effects against certain prion strains.
  • Limitations exist: compounds are ineffective for some prion strains (e.g., 263K) and prion diseases without amyloid plaques.

Conclusions:

  • Amyloid-binding compounds offer potential for prion disease diagnosis and therapy, with specific examples showing promise.
  • The efficacy of these compounds is strain- and disease-dependent, highlighting the need for further research.
  • Clarifying the atomic-level binding interactions is crucial to overcome current limitations and expand therapeutic applications.