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Amyloid Fibrils03:03

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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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A Rigid Supramolecular Solution to a Flexible Problem: A Multifunctional Calix[4]arene-Based Strategy to Prevent

Davide Dell'Accantera1, Giulia Piccinini1, Cristina Ciabini2

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A novel supramolecular strategy using CLXP1 effectively inhibits alpha-synuclein aggregation, a key factor in Parkinson's disease. This approach reduces cellular toxicity and offers a promising therapeutic avenue for synucleinopathies.

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Area of Science:

  • Biochemistry
  • Neuroscience
  • Supramolecular Chemistry

Background:

  • Pathological aggregation of alpha-synuclein (syn) is central to Parkinson's disease (PD) and synucleinopathies.
  • Developing strategies to inhibit syn aggregation and associated toxicity is crucial for PD treatment.

Purpose of the Study:

  • To investigate a supramolecular host-guest chemistry approach using anionic calix[4]-arenes to inhibit syn aggregation.
  • To evaluate the efficacy of CLXP1, a specific calix[4]-arene derivative, in reducing syn aggregation and cellular toxicity in a PD model.

Main Methods:

  • Design and synthesis of anionic calix[4]-arenes as syn aggregation inhibitors.
  • Utilized a yeast model overexpressing syn to validate PD pathology.
  • Employed cell viability assays, NMR spectroscopy, and analysis of molecular pathways, mitochondrial morphology, homeostasis, and autophagy.

Main Results:

  • CLXP1 demonstrated potent inhibition of syn aggregation in the yeast PD model.
  • CLXP1 significantly enhanced cell viability by reducing toxic syn inclusions.
  • CLXP1 preserved mitochondrial function, restored homeostasis, and promoted autophagic clearance.

Conclusions:

  • CLXP1 stabilizes the alpha-helical, membrane-bound conformation of syn, preventing toxic oligomerization.
  • Supramolecular host-guest chemistry offers a viable strategy for targeting intrinsically disordered proteins like syn.
  • CLXP1 serves as a promising scaffold for developing novel modulators of protein aggregation for synucleinopathies.