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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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Functional groups are a group of atoms with characteristic properties, which when linked to the carbon skeleton of a molecule, alter the properties of that molecule. For example, the presence of certain functional groups on a molecule will make them hydrophilic, whereas others will make them hydrophobic. These functional groups are an indispensable part of organic chemistry and important components of biological molecules, such as carbohydrates, proteins, lipids, and nucleic acids. Each...
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Rapid Generation of Amyloid from Native Proteins In vitro
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Functional Amyloids.

Daniel Otzen1, Roland Riek2

  • 1iNANO, Aarhus University, DK-8000 Aarhus C, Denmark.

Cold Spring Harbor Perspectives in Biology
|May 16, 2019
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Summary
This summary is machine-generated.

Amyloids, known for disease, also serve crucial functions in nature. This review explores functional amyloids in bacteria, fungi, and mammals, highlighting their diverse roles beyond disease association.

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Area of Science:

  • Biochemistry
  • Molecular Biology
  • Structural Biology

Background:

  • Proteins and peptides aggregate into amyloid structures, characterized by cross-β-sheet fibrils.
  • While often linked to diseases like Alzheimer's, amyloids possess inherent stability and replication mechanisms.
  • Nature utilizes amyloid structures for diverse biological roles across various organisms.

Purpose of the Study:

  • To review the multifaceted roles of functional amyloids in biological systems.
  • To highlight the structural, reservoir, information carrier, and signaling functions of amyloids.
  • To differentiate between functional and disease-associated amyloid formations.

Main Methods:

  • Literature review of scientific articles on functional amyloids.
  • Focus on specific amyloid systems: bacterial curli, fungal HET-s prion, and mammalian peptide hormone storage.
  • Comparative analysis of functional and disease-associated amyloids.

Main Results:

  • Functional amyloids are involved in structure formation (biofilms, hyphae), storage (peptide hormones), information transfer (prions, memory), and signaling.
  • Examples include bacterial curli for biofilms, fungal HET-s for immunity, and peptide hormones in secretory granules.
  • Amyloid structures exhibit high stability and self-replication, enabling their diverse biological applications.

Conclusions:

  • Functional amyloids are essential biological components with diverse roles beyond pathological aggregates.
  • Understanding functional amyloids provides insights into protein aggregation mechanisms and potential therapeutic strategies.
  • Distinguishing functional from disease-associated amyloids is crucial for comprehending their biological significance.