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Related Concept Videos

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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Proteins are polymers of amino acid residues. They are versatile and responsible for different cellular functions, including DNA replication, molecular transport, catalysis, and structural support. Proteins have a hierarchical structure comprising at least three levels of organization: primary, secondary, and tertiary structure. Some large proteins have a quaternary structure where individual protein subunits are linked together.
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Proteins are chains of amino acids linked together by peptide bonds. Upon synthesis, a protein folds into a three-dimensional conformation, critical to its biological function. Interactions between its constituent amino acids guide protein folding, and hence the protein structure is primarily dependent on its amino acid sequence.
Protein Structure Is Critical to Its Biological Function
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Structure and Aggregation Mechanisms in Amyloids.

Zaida L Almeida1, Rui M M Brito1

  • 1Chemistry Department and Coimbra Chemistry Centre, Faculty of Sciences and Technology, University of Coimbra, 3004-535 Coimbra, Portugal.

Molecules (Basel, Switzerland)
|March 12, 2020
PubMed
Summary
This summary is machine-generated.

Amyloid diseases like Alzheimer's stem from protein misfolding and aggregation into fibrils. Understanding amyloid structure and formation is key to developing effective therapies for these debilitating conditions.

Keywords:
aggregatesaggregationaggregation mechanismsamyloid dyesamyloid fibrilsamyloid structureamyloidosismisfolding diseasesoligomerssteric zipper

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Area of Science:

  • Biochemistry
  • Molecular Biology
  • Neuroscience

Background:

  • Amyloid diseases arise from polypeptide chain aggregation into fibrils, forming plaques and inclusions.
  • Over 50 amyloid diseases, including Alzheimer's and Parkinson's, are known, impacting millions globally.
  • Identifying critical molecular species in amyloid formation is crucial for understanding disease progression.

Purpose of the Study:

  • To review current knowledge on amyloid fibril formation, structure, and cytotoxicity.
  • To explore the kinetic and thermodynamic aspects of the amyloid cascade.
  • To provide insights for developing rational therapeutic strategies against amyloid diseases.

Main Methods:

  • Utilized X-ray and electron diffraction for structural analysis.
  • Employed solid-state nuclear magnetic resonance spectroscopy (ssNMR) to study amyloid structures.
  • Applied cryo-electron microscopy (cryo-EM) to visualize amyloid fibril morphology.

Main Results:

  • Amyloid structures generally conform to the cross-β amyloid motif.
  • Revealed a diversity of polymorphic structures within amyloid fibrils.
  • Highlighted the importance of understanding molecular mechanisms for therapeutic development.

Conclusions:

  • A comprehensive understanding of amyloid formation kinetics, thermodynamics, and structure is essential.
  • Elucidating the origin of cytotoxicity is critical for targeting amyloid diseases.
  • This review consolidates current knowledge to guide future research and therapeutic interventions.