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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. 
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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Amyloid Fibrils03:03

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Factors Affecting Dissolution: Polymorphism, Amorphism and Pseudopolymorphism01:21

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Polymorphism refers to the existence of a drug substance in multiple crystalline forms, known as polymorphs. Recently, this term has been expanded to include solvates (forms containing a solvent), amorphous forms (non-crystalline forms), and desolvated solvates (forms from which the solvent has been removed).
Some polymorphic crystals possess lower aqueous solubility than their amorphous counterparts, leading to incomplete absorption. For instance, the oral suspension of Chloramphenicol, which...
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Interactions with and Membrane Permeabilization of Brain Mitochondria by Amyloid Fibrils
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Amyloid Fibril Solubility.

L G Rizzi1, S Auer1

  • 1School of Chemistry, University of Leeds , Leeds LS2 9JT, United Kingdom.

The Journal of Physical Chemistry. B
|October 27, 2015
PubMed
Summary
This summary is machine-generated.

Researchers explored amyloid fibril solubility using simulations. They found solubility depends on fibril thickness and inter-protein interactions, offering insights for designing protein aggregation properties.

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Area of Science:

  • Biophysics
  • Computational Biology
  • Materials Science

Background:

  • Amyloid fibril solubility is protein-specific.
  • The relationship between inter-protein interactions and fibril solubility is not well understood.

Purpose of the Study:

  • To investigate how interactions between fibril building blocks influence amyloid fibril solubility.
  • To develop a predictive model for amyloid fibril solubility based on inter-protein interactions.

Main Methods:

  • Utilized a simple protein model for Monte Carlo simulations.
  • Directly measured amyloid fibril solubility as a function of inter-protein interactions.

Main Results:

  • Confirmed that amyloid fibril solubility is dependent on fibril thickness.
  • Established an analytical formula describing the relationship between inter-protein interactions and solubility.
  • Identified general rules for how side-chain interactions, hydrogen bonding, and temperature affect solubility.

Conclusions:

  • Developed a simulation-based approach to understand and predict amyloid fibril solubility.
  • The findings provide a foundation for designing protein fibrils with controlled solubility and aggregation characteristics.