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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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An In Vitro Model for Studying Tau Aggregation Using Lentiviral-mediated Transduction of Human Neurons
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Modulation of tau protein aggregation using 'Trojan' sequences.

Gaurav Pandey1, Sudhir Morla1, Sachin Kumar1

  • 1Department of Biosciences and Bioengineering, Indian Institute of Technology Guwahati, Guwahati 781039, India.

Biochimica Et Biophysica Acta. General Subjects
|March 2, 2020
PubMed
Summary
This summary is machine-generated.

Researchers designed novel Trojan peptides to target tau protein aggregation, a hallmark of tauopathies. These peptides show potential for treating neurodegenerative diseases by modulating fibril formation and reducing neurotoxicity.

Keywords:
AmyloidsPeptide-based inhibitorsTauTaupathiesVQIVYK

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Area of Science:

  • Neuroscience
  • Biochemistry
  • Drug Discovery

Background:

  • Tauopathies are a group of over 30 neurodegenerative disorders linked to abnormal tau protein assembly into neurofibrillary tangles.
  • Millions are affected worldwide, with current therapies offering limited symptomatic relief, highlighting an urgent need for effective treatments.

Purpose of the Study:

  • To design and evaluate novel peptide-based perturbants (Trojans) for modulating tau protein aggregation.
  • To assess the efficacy of these peptides in preventing or reversing the formation of toxic tau aggregates.

Main Methods:

  • Employed a structure-based design approach to create short peptide perturbants targeting tau's hydrophobic core.
  • Utilized biophysical methods, serum stability, toxicity, and blood-brain barrier (BBB) assays to evaluate peptide efficacy.

Main Results:

  • Trojan peptides modulated the aggregation of a tau peptide fragment, either accelerating or arresting self-assembly.
  • Designed peptides demonstrated negligible cytotoxicity, high serum stability, and BBB permeability.
  • Trojans were capable of disassembling pre-formed tau fibrillar assemblies and reducing associated neurotoxicity.

Conclusions:

  • Designed Trojan peptides show potential as a therapeutic strategy for tauopathies.
  • These peptides can modulate tau aggregation at pre- and post-assembly stages, offering a novel therapeutic avenue.