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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...
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...

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Related Experiment Video

Updated: Jul 11, 2026

A11-positive &#946;-amyloid Oligomer Preparation and Assessment Using Dot Blotting Analysis
06:17

A11-positive β-amyloid Oligomer Preparation and Assessment Using Dot Blotting Analysis

Published on: May 22, 2018

Polyfluorinated bis-styrylbenzene beta-amyloid plaque binding ligands.

Daniel P Flaherty1, Shannon M Walsh, Tomomi Kiyota

  • 1University of Nebraska Medical Center, College of Pharmacy, 986025 Nebraska Medical Center, Omaha, Nebraska 68198, USA.

Journal of Medicinal Chemistry
|September 12, 2007
PubMed
Summary

New bis-styrylbenzene compounds show enhanced binding to beta-amyloid (Abeta) peptides. These findings pave the way for developing noninvasive Alzheimer's disease detection tools using 19F MRI.

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Imaging Amyloid Tissues Stained with Luminescent Conjugated Oligothiophenes by Hyperspectral Confocal Microscopy and Fluorescence Lifetime Imaging
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Imaging Amyloid Tissues Stained with Luminescent Conjugated Oligothiophenes by Hyperspectral Confocal Microscopy and Fluorescence Lifetime Imaging

Published on: October 20, 2017

Area of Science:

  • Organic Chemistry
  • Neuroscience
  • Biochemistry

Background:

  • Alzheimer's disease (AD) is characterized by the aggregation of beta-amyloid (Abeta) peptides.
  • Developing sensitive and specific probes for Abeta detection is crucial for early AD diagnosis.
  • Fluorinated organic compounds offer unique properties for molecular imaging and diagnostics.

Purpose of the Study:

  • To synthesize and characterize novel bis-styrylbenzene derivatives with varying fluorination patterns.
  • To evaluate the binding affinities and specificities of these compounds to Abeta peptides.
  • To assess the potential of these compounds as noninvasive imaging agents for Alzheimer's disease.

Main Methods:

  • Synthesis of six bis-styrylbenzene derivatives with tetrafluorophenyl cores or trifluoromethyl/trifluoromethoxy groups.
  • Fluorescence titrations using Abeta1-40 peptide to determine binding affinities.
  • In vitro fluorescence-based assay using brain sections from APP/PS1 transgenic mice.
  • Evaluation of blood-brain barrier penetration capabilities.

Main Results:

  • Bis-styrylbenzenes with tetrafluorophenyl cores exhibited significantly higher Abeta binding affinities than phenyl or monofluorophenyl analogs.
  • Compounds with carboxylic acid functional groups showed lower Abeta binding affinities compared to neutral counterparts.
  • Selected bis-styrylbenzenes demonstrated effective blood-brain barrier penetration.

Conclusions:

  • The study establishes structure-activity relationships (SAR) for bis-styrylbenzene binding to Abeta.
  • Fluorination, particularly tetrafluorophenyl cores, enhances Abeta binding affinity.
  • These findings support the development of novel fluorinated probes for noninvasive Alzheimer's disease detection via 19F MRI.