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Related Concept Videos

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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. 
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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...
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Updated: Apr 23, 2026

Generation of Alpha-Synuclein Preformed Fibrils from Monomers and Use In Vivo
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Angelic Acid Disassembles Fibrillar α-Synuclein Aggregates through β-Sheet Interface Disruption.

Hyo Gi Jung1, Junho Bang1,2,3, Juhyun Kim4

  • 1School of Biomedical Engineering, College of Health Science, Korea University, 145 Anam-ro, Seongbuk-gu, Seoul 02841, Republic of Korea.

ACS Chemical Neuroscience
|April 21, 2026
PubMed
Summary
This summary is machine-generated.

Angelic acid effectively disassembles pathological alpha-synuclein fibrils, reducing neurotoxic protein accumulation and cytotoxicity in cellular models of synucleinopathies like Parkinson's disease.

Keywords:
angelic acidfibril disassemblynatural productplasmonic nanoparticle amyloid corona (PNAC)synucleinopathiesα-synuclein

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Area of Science:

  • Neuroscience
  • Biochemistry
  • Pharmacology

Background:

  • Pathological aggregation of alpha-synuclein (αS) is a key feature of synucleinopathies, including Parkinson's disease.
  • Fibrillar αS aggregates are implicated in driving neurodegeneration in these conditions.

Purpose of the Study:

  • To identify small molecules that can disassemble fibrillar αS aggregates.
  • To evaluate the therapeutic potential of identified compounds for synucleinopathies.

Main Methods:

  • Screening of a natural product library using a plasmonic nanoparticle amyloid corona platform.
  • Physicochemical property analysis for cell permeability and CNS accessibility.
  • Characterization of αS fibril disruption using spectroscopy and microscopy.
  • In vitro cell-based assays to assess αS reduction and cytotoxicity.

Main Results:

  • Angelic acid was identified as a top candidate for its ability to disrupt β-sheet rich conformations and fragment αS fibrils.
  • Molecular docking suggested interactions between angelic acid and αS fibril interfaces.
  • Angelic acid significantly reduced intracellular αS accumulation (up to 91.4%) and alleviated αS fibril-induced cytotoxicity (34.1%) in a cellular model.

Conclusions:

  • Angelic acid demonstrates potent αS-targeting activity, reducing toxic aggregates and cytotoxicity.
  • Angelic acid represents a promising lead compound for synucleinopathy treatment.
  • Further in vivo studies are warranted to evaluate angelic acid's efficacy in synucleinopathy models.