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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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A Tripeptide-Stabilized Nanoemulsion of Oleic Acid
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Nanoparticles in relation to peptide and protein aggregation.

Masihuz Zaman1, Ejaz Ahmad1, Atiyatul Qadeer1

  • 1Interdisciplinary Biotechnology Unit, Aligarh Muslim University, Aligarh, India.

International Journal of Nanomedicine
|March 11, 2014
PubMed
Summary

Nanoparticles influence protein and peptide aggregation, impacting amyloid formation. This review explores how nanoparticles can induce or inhibit fibrillation and disaggregate fibrils, considering their formulation and toxicity.

Keywords:
amyloid formationinducerinhibitornanoparticlenucleationtoxicity

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Area of Science:

  • Biomaterials Science
  • Nanotechnology
  • Biochemistry

Background:

  • Protein and peptide aggregation are implicated in amyloid-related diseases.
  • Nanoparticles offer unique properties (small size, high surface area) for studying these processes.
  • Understanding nanoparticle interactions with proteins is crucial for therapeutic development.

Purpose of the Study:

  • To review the dual role of nanoparticles in protein and peptide fibrillation: as inducers and inhibitors.
  • To explore nanoparticle effects on nucleation kinetics and the disaggregation of preformed fibrils.
  • To discuss nanoparticle formulation, characterization, and toxicological profiles.

Main Methods:

  • Literature review of studies investigating nanoparticle-protein interactions.
  • Analysis of nanoparticle composition, surface properties, and concentration effects.
  • Examination of thermodynamic parameters governing fibrillation and disaggregation.

Main Results:

  • Nanoparticle effects on fibrillation are dependent on particle composition, surface characteristics, and concentration.
  • Nanoparticles can modulate nucleation kinetics, either promoting or inhibiting amyloid formation.
  • Certain nanoparticles demonstrate potential for disaggregating preformed amyloid fibrils.

Conclusions:

  • Nanoparticles represent a versatile tool for controlling protein and peptide aggregation in amyloid-related diseases.
  • Careful consideration of nanoparticle formulation and characterization is essential for targeted applications.
  • Further research into the in vivo and in vitro toxicological effects of nanoparticles is warranted.