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Updated: Jun 10, 2026

Generation of Alpha-Synuclein Preformed Fibrils from Monomers and Use In Vivo
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Quantifying prefibrillar amyloids in vitro by using a "thioflavin-like" spectroscopic method.

Ashley A Reinke1, Gelareh A Abulwerdi, Jason E Gestwicki

  • 1Department of Pathology, University of Michigan, 4000 Life Sciences Institute, 210 Washtenaw Avenue, Ann Arbor, MI 48109-2216, USA.

Chembiochem : a European Journal of Chemical Biology
|August 3, 2010
PubMed
Summary

Researchers developed a new fluorescent probe, tryptophanol (TROL), to specifically detect toxic prefibrillar amyloid structures. This method, combined with thioflavin T (ThT), offers better insights into amyloid formation in neurodegenerative diseases.

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Area of Science:

  • Biochemistry
  • Neuroscience
  • Biophysics

Background:

  • Protein aggregates, including fibrils and prefibrillar structures, are implicated in neurodegenerative diseases like Alzheimer's.
  • Prefibrillar amyloid aggregates are highly neurotoxic and correlate with cognitive impairment.
  • Current methods like thioflavin T (ThT) lack specificity for distinguishing between aggregate types.

Purpose of the Study:

  • To identify a novel fluorescent probe that selectively quantifies prefibrillar amyloid structures.
  • To develop an improved spectroscopic assay for amyloid detection.
  • To investigate the dynamics of amyloid-beta (Abeta) aggregation using the new probe.

Main Methods:

  • Screening of 37 indoles to find a selective fluorescent probe for prefibrillar Abeta.

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  • Development of a quantitative assay using tryptophanol (TROL) and thioflavin T (ThT).
  • Utilizing electron microscopy to validate probe findings and analyze aggregation kinetics.

    • Main Results:

    • Tryptophanol (TROL) was identified as a selective probe for prefibrillar amyloid structures.
    • The TROL assay, combined with ThT, revealed that prefibrils persist even after ThT signal saturation during Abeta aggregation.
    • TROL demonstrated cross-reactivity with other amyloid-prone proteins, including ataxin-3, amylin, and CsgA.

    Conclusions:

    • A combination of TROL and ThT provides enhanced insight into Abeta amyloid formation.
    • The TROL assay offers a potentially inexpensive spectroscopic method for quantifying amyloid prefibrils in vitro.
    • This approach may be applicable to studying other amyloidogenic proteins relevant to various diseases.