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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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Neural Regulation01:37

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Digestion begins with a cephalic phase that prepares the digestive system to receive food. When our brain processes visual or olfactory information about food, it triggers impulses in the cranial nerves innervating the salivary glands and stomach to prepare for food.
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In complexation reactions, metal cations are the electron pair acceptors, and the ligands are the electron pair donors. The stability of the metal complexes depends primarily on the complexing ability of the central metal ion and the nature of the ligands. Generally, the complexing ability of the metal ion depends on the size and charge of the ion. As the metal ion size increases, the stability of the metal complexes decreases, provided that the valency of the metal ion and the ligands remain...
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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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Related Experiment Video

Updated: Mar 26, 2026

A Method to Study α-Synuclein Toxicity and Aggregation Using a Humanized Yeast Model
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Alpha-synuclein: relating metals to structure, function and inhibition.

J S McDowall1, D R Brown

  • 1Department of Biology and Biochemistry, University of Bath, Claverton Down, Bath, BA2 7AY, UK. bssdrb@bath.ac.uk.

Metallomics : Integrated Biometal Science
|February 12, 2016
PubMed
Summary

Alpha-synuclein

Area of Science:

  • Neuroscience
  • Molecular Biology
  • Biochemistry

Background:

  • Alpha-synuclein's role in Parkinson's disease (PD) pathogenesis is recognized, yet its precise function remains unclear.
  • The protein's structural plasticity is crucial for normal cellular activity and PD progression.
  • Oligomeric species formation in the substantia nigra correlates with PD advancement, with partially folded intermediates potentially initiating fibrillization.

Purpose of the Study:

  • To explore the structural plasticity of alpha-synuclein.
  • To investigate the influence of factors like mutations, metals, and neurotransmitters on alpha-synuclein structure.
  • To examine the implications of alpha-synuclein's potential ferrireductase activity in neurodegeneration.

Main Methods:

  • Analysis of alpha-synuclein structure and function.

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Interactions with and Membrane Permeabilization of Brain Mitochondria by Amyloid Fibrils
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  • Investigating interactions with dopamine and metal ions.
  • Evaluating the protein's ferrireductase activity.

    • Main Results:

    • Alpha-synuclein exhibits significant structural plasticity.
    • Dopamine and metal interactions in the substantia nigra can alter alpha-synuclein structure.
    • Alpha-synuclein may act as a ferrireductase, catalyzing reactive oxygen species formation.

    Conclusions:

    • Alpha-synuclein's structural plasticity is central to its function and role in PD.
    • The substantia nigra environment promotes alpha-synuclein alterations and oxidative stress.
    • Alpha-synuclein's ferrireductase activity could be a key mechanism driving neurodegeneration in Parkinson's disease.