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Related Concept Videos

Molecular Chaperones and Protein Folding03:00

Molecular Chaperones and Protein Folding

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The native conformation of a protein is formed by interactions between the side chains of its constituent amino acids. When the amino acids cannot form these interactions, the protein cannot fold by itself and needs chaperones. Notably, chaperones do not relay any additional information required for the folding of polypeptides; the native conformation of a protein is determined solely by its amino acid sequence. Chaperones catalyze protein folding without being a part of the folded protein.
The...
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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. 
Amyloid deposits were observed as early as 1639 in the liver and the spleen.   In 1854, Rudolph Virchow performed iodine staining,...
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Bacterial Protein Maturation01:26

Bacterial Protein Maturation

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Bacterial protein maturation is a tightly regulated process that ensures newly synthesized polypeptides achieve correct functional conformations. This maturation involves a series of modifications, folding events, and quality control steps, often assisted by specialized chaperone proteins.N-Terminal ModificationsThe maturation of bacterial polypeptides begins cotranslationally as the polypeptide exits the ribosome. The first amino acid, N-formylmethionine (fMet), is typically modified at the...
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Protein Folding01:25

Protein Folding

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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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Export of Misfolded Proteins out of the ER01:32

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After folding, the ER assesses the quality of secretory and membrane proteins. The correctly folded proteins are cleared by the calnexin cycle for transport to their final destination, while misfolded proteins are held back in the ER lumen. The ER chaperones attempt to unfold and refold the misfolded proteins but sometimes fail to achieve the correct native conformation. Such terminally misfolded proteins are then exported to the cytosol by ER-associated degradation or ERAD pathway for...
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Protein Folding Quality Check in the RER01:29

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ER is the primary site for the maturation and folding of soluble and transmembrane secretory proteins. The calnexin cycle is a specific chaperone system that folds and assesses the confirmation of N-glycosylated proteins before they can exit the ER lumen. The primary players of this quality check pipeline are the lectins, ER-resident chaperones, and a glucosyl transferase enzyme. In case the calnexin system in the lumen fails to salvage a misfolded protein, it is transported to the cytoplasm...
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Related Experiment Video

Updated: Aug 16, 2025

Characterization of pH-Dependent Reversible Self-Assembly of Amyloid Beta 1-40-Coated Gold Colloids
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Characterization of pH-Dependent Reversible Self-Assembly of Amyloid Beta 1-40-Coated Gold Colloids

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Amyloid Disassembly: What Can We Learn from Chaperones?

Zaida L Almeida1, Rui M M Brito1

  • 1Chemistry Department and Coimbra Chemistry Centre-Institute of Molecular Sciences (CQC-IMS), University of Coimbra, 3004-535 Coimbra, Portugal.

Biomedicines
|December 23, 2022
PubMed
Summary

Amyloid diseases involve toxic protein aggregates. This review explores chemical and biochemical agents, including molecular and pharmacological chaperones, that can disaggregate these harmful amyloids, offering potential therapeutic strategies for amyloidosis.

Keywords:
aberrant aggregatesamyloid disassemblyamyloid fibrilsamyloidosischemical chaperonesdisaggregasesmolecular chaperonespharmacological chaperonesprotein aggregationprotein misfolding

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Area of Science:

  • Biochemistry
  • Molecular Biology
  • Neuroscience

Background:

  • Amyloid diseases are characterized by protein aggregation into insoluble fibrils.
  • Soluble oligomers and fibrils are cytotoxic, causing cell death and organ dysfunction.
  • Neurodegenerative diseases like Alzheimer's and Parkinson's are linked to amyloid pathologies.

Purpose of the Study:

  • To review chemical and biochemical agents capable of disaggregating preformed amyloids.
  • To analyze the mode of action, structure, and interactions of these disaggregation agents.
  • To evaluate the potential of disaggregation agents as a therapeutic strategy for amyloidosis.

Main Methods:

  • Literature compilation of chemical and biochemical agents.
  • Classification of agents into molecular chaperones, chemical chaperones, and pharmacological chaperones.
  • Focus on agents' mechanism, structure, and disaggregation products.

Main Results:

  • Identified various agents that can disaggregate amyloid fibrils.
  • Detailed the properties and interactions of these disaggregation agents.
  • Assessed the morphology and toxicity of disaggregation products.

Conclusions:

  • Amyloid fibril disassembly is a promising disease-modifying strategy.
  • Disaggregation agents, including chaperones, show potential for treating amyloidosis.
  • Further research into these agents could improve patient outcomes and quality of life.