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Related Concept Videos

Amyloid Fibrils03:03

Amyloid Fibrils

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, normally used to...
Structure of Amines01:19

Structure of Amines

The hybridized nitrogen atom in amines possesses a lone pair of electrons and is bound to three substituents with a bond angle of around 108°, which is less than the tetrahedral angle of 109.5°. However, the C–N–H bond angle is slightly larger at 112°, with a carbon–nitrogen bond length of 147 pm. This carbon–nitrogen bond length of of amines is longer than the carbon–oxygen bond of alcohols (143 pm) but shorter than alkanes’ carbon–carbon bond (154 pm). These aspects are illustrated in Figure...
Protein Complexes with Interchangeable Parts01:57

Protein Complexes with Interchangeable Parts

Groups of proteins may form a complex where each protein in this complex has a different role in the overall execution of the complex’s function. Often some of the proteins in the complex can be replaced by a closely related variant to give a complex that contains many of the same components yet is functionally distinct.
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Protein Complex Assembly02:41

Protein Complex Assembly

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Many viruses self-assemble into a fully functional unit using the infected host cell to...

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Related Experiment Video

Updated: Jun 20, 2026

Screening for Amyloid Aggregation by Semi-Denaturing Detergent-Agarose Gel Electrophoresis
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Screening for Amyloid Aggregation by Semi-Denaturing Detergent-Agarose Gel Electrophoresis

Published on: July 16, 2008

Complex polyamines: unique prion disaggregating compounds.

Surachai Supattapone1, Justin R Piro, Judy R Rees

  • 1Department of Biochemistry, Dartmouth Medical School, Hanover, New Hampshire 03755, USA. supattapone@dartmouth.edu

CNS & Neurological Disorders Drug Targets
|August 26, 2009
PubMed
Summary
This summary is machine-generated.

Complex polyamines, like cationic dendrimers, are promising anti-prion agents that remove disease-causing PrP(Sc) proteins. Future research focuses on safe delivery of these potent compounds to the brain.

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Investigating the Spreading and Toxicity of Prion-like Proteins Using the Metazoan Model Organism C. elegans
12:57

Investigating the Spreading and Toxicity of Prion-like Proteins Using the Metazoan Model Organism C. elegans

Published on: January 8, 2015

Area of Science:

  • Biochemistry and Molecular Biology
  • Neuroscience
  • Pharmacology

Background:

  • Prion diseases are neurodegenerative disorders caused by misfolded prion proteins (PrPSc).
  • Complex polyamines, particularly cationic dendrimers, show potential as anti-prion chemotherapeutic agents.
  • These compounds are unique in their ability to remove existing PrPSc from infected cells.

Purpose of the Study:

  • To investigate the mechanism of action of complex polyamines, specifically cationic dendrimers, in disaggregating PrPSc.
  • To explore the potential of dendrimers and related compounds as therapeutic agents for prion diseases and other protein misfolding disorders.
  • To identify challenges and future research directions for developing these agents for central nervous system delivery.

Main Methods:

  • Examined the relationship between polyamine charge density and anti-prion potency.
  • Investigated the cellular localization of cationic dendrimers and PrPSc in lysosomes.
  • Assessed the disaggregation capabilities of dendrimers on various amyloid proteins and model peptides.

Main Results:

  • Cationic dendrimer potency correlates with surface positive charge density.
  • Dendrimers accumulate with PrPSc in lysosomes, where acidic pH aids PrPSc disaggregation.
  • Dendrimers can disaggregate amyloid proteins and potentially inhibit fiber formation.
  • Lipopolyamines, a related class, possess a lipophilic tail for potential membrane targeting.

Conclusions:

  • Complex polyamines, especially cationic dendrimers, demonstrate significant potential for clearing PrPSc and disaggregating amyloid proteins.
  • Challenges include poor bioavailability, limited activity spectrum, and potential neurological side effects.
  • Developing safe strategies for central nervous system delivery of these compounds is crucial for therapeutic advancement.