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Amyloid Fibrils03:03

Amyloid Fibrils

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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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Metal-Ligand Bonds02:51

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The hemoglobin in the blood, the chlorophyll in green plants, vitamin B-12, and the catalyst used in the manufacture of polyethylene all contain coordination compounds. Ions of the metals, especially the transition metals, are likely to form complexes.
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A type of Lewis acid-base chemistry involves the formation of a complex ion (or a coordination complex) comprising a central atom, typically a transition metal cation, surrounded by ions or molecules called ligands. These ligands can be neutral molecules like H2O or NH3, or ions such as CN− or OH−. Often, the ligands act as Lewis bases, donating a pair of electrons to the central atom. These types of Lewis acid-base reactions are examples of a broad subdiscipline called coordination...
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A11-positive &#946;-amyloid Oligomer Preparation and Assessment Using Dot Blotting Analysis
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Metal ions control amyloid catalysis.

Fiamma Ayelen Buratti1, Ranjeet Kumar2, Pernilla Wittung-Stafshede1

  • 1Rice University, Department of Chemistry, Houston, 77005, TX, USA.

Journal of Inorganic Biochemistry
|October 18, 2025
PubMed
Summary
This summary is machine-generated.

Pathological amyloids, like alpha-synuclein in Parkinson's disease, can catalyze reactions. Divalent metal ions, copper (Cu(II)) and zinc (Zn(II)), modulate this activity, impacting adenosine triphosphate (ATP) hydrolysis and binding.

Keywords:
AmyloidCatalytic activityHydrolysisMetal ionsParkinsonα-synuclein

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Area of Science:

  • Biochemistry
  • Neuroscience
  • Protein Chemistry

Background:

  • Pathological amyloids, such as alpha-synuclein aggregates in Parkinson's disease, exhibit catalytic activity.
  • Metal ion dysregulation is common in neurodegenerative disorders.
  • Amyloidogenic proteins often bind metal ions, suggesting potential in vivo interactions.

Purpose of the Study:

  • To investigate the modulatory effects of copper (Cu(II)) and zinc (Zn(II)) on the catalytic activity of alpha-synuclein amyloids.
  • To determine how these metal ions influence adenosine triphosphate (ATP) hydrolysis and binding by alpha-synuclein amyloids.
  • To assess the impact of specific mutations (H50A) and metal ions on lipase and esterase activities of alpha-synuclein amyloids.

Main Methods:

  • Formation of alpha-synuclein amyloids with and without Cu(II) and Zn(II).
  • Assessment of amyloid catalytic activity towards adenosine triphosphate (ATP) dephosphorylation.
  • Measurement of ATP binding using fluorescent analogs.
  • Evaluation of lipase activity on a model substrate.
  • Hydrolysis assays using para-nitrophenyl acetate (pNPA).

Main Results:

  • Zinc (Zn(II)) significantly inhibits the catalytic activity and ATP binding of alpha-synuclein amyloids.
  • Copper (Cu(II)) retains or restores catalytic activity and ATP binding, even in the H50A mutant.
  • Lipase activity is unaffected by Cu(II) but abolished by Zn(II) for both wild-type and H50A amyloids.
  • Para-nitrophenyl acetate (pNPA) hydrolysis is insensitive to metal ions and the H50A mutation.

Conclusions:

  • Divalent metal ions, particularly Zn(II) and Cu(II), play a crucial role in modulating the catalytic functions of alpha-synuclein amyloids.
  • The findings suggest that metal ion-dependent modulation of amyloid catalysis could be relevant in the context of neurodegenerative diseases.
  • Understanding these interactions is vital for deciphering the in vivo roles of amyloids and associated metal ions.