Jove
Visualize
Contact Us
JoVE
x logofacebook logolinkedin logoyoutube logo
ABOUT JoVE
OverviewLeadershipBlogJoVE Help Center
AUTHORS
Publishing ProcessEditorial BoardScope & PoliciesPeer ReviewFAQSubmit
LIBRARIANS
TestimonialsSubscriptionsAccessResourcesLibrary Advisory BoardFAQ
RESEARCH
JoVE JournalMethods CollectionsJoVE Encyclopedia of ExperimentsArchive
EDUCATION
JoVE CoreJoVE BusinessJoVE Science EducationJoVE Lab ManualFaculty Resource CenterFaculty Site
Terms & Conditions of Use
Privacy Policy
Policies

Related Concept Videos

Labeling DNA Probes03:31

Labeling DNA Probes

9.1K
DNA probes are fragments of DNA labeled with a reporter tag to enable their detection or purification. The resulting labeled DNA probes can then hybridize to target nucleic acid sequences through complementary base-pairing, and may be used to recover or identify these regions.
Radioisotopes, fluorophores, or small molecule binding partners like biotin or digoxigenin, are the most widely used reporter tags for labeling DNA probes. These labels can be attached to the probe DNA molecule via...
9.1K

You might also read

Related Articles

Articles linked to this work by shared authors, journal, and citation graph.

Sort by
Same author

Genetic Code Expansion for Site-Specific Encoding of a Switchable, Intrinsic Fluorophore-Quencher Pair to Monitor Protein Dynamics.

bioRxiv : the preprint server for biology·2026
Same author

Genetic Code Expansion, Enzymatic Modification, and C-Terminal Labeling Enable Facile Production of Highly Modified α-Synuclein.

bioRxiv : the preprint server for biology·2026
Same author

Brain-gut axis imaging, motion correction with [ <sup>11</sup> C]-carfentanil total-body PET.

medRxiv : the preprint server for health sciences·2026
Same author

Stabilized thioamide peptide agonists of the neuropeptide Y type 2 receptor for targeted cancer imaging.

RSC chemical biology·2026
Same author

Determination of α-Synuclein Protein Interactions by μMap Photoproximity Labeling.

Journal of the American Chemical Society·2026
Same author

Machine learning prediction of multiple distinct high-affinity chemotypes for α-synuclein fibrils.

Chemical communications (Cambridge, England)·2026

Related Experiment Video

Updated: Dec 27, 2025

Utilizing Time-Resolved Protein-Induced Fluorescence Enhancement to Identify Stable Local Conformations One &#945;-Synuclein Monomer at a Time
07:56

Utilizing Time-Resolved Protein-Induced Fluorescence Enhancement to Identify Stable Local Conformations One α-Synuclein Monomer at a Time

Published on: May 30, 2021

3.5K

Synthesis and characterization of high affinity fluorogenic α-synuclein probes.

Zsofia Lengyel-Zhand1, John J Ferrie2, Bieneke Janssen1

  • 1Department of Radiology, Perelman School of Medicine, University of Pennsylvania, Philadelphia, PA 19104, USA. rmach@pennmedicine.upenn.edu.

Chemical Communications (Cambridge, England)
|February 28, 2020
PubMed
Summary

Researchers developed novel benzofuranone-based fluorescent probes to image alpha-synuclein (α-synuclein) pathology. These probes exhibit specific binding and fluorescence turn-on, aiding in understanding synucleinopathies.

More Related Videos

Studying Pre-formed Fibril Induced &#945;-Synuclein Accumulation in Primary Embryonic Mouse Midbrain Dopamine Neurons
10:03

Studying Pre-formed Fibril Induced α-Synuclein Accumulation in Primary Embryonic Mouse Midbrain Dopamine Neurons

Published on: August 16, 2020

11.1K
Generation of Alpha-Synuclein Preformed Fibrils from Monomers and Use In Vivo
09:44

Generation of Alpha-Synuclein Preformed Fibrils from Monomers and Use In Vivo

Published on: June 2, 2019

22.3K

Related Experiment Videos

Last Updated: Dec 27, 2025

Utilizing Time-Resolved Protein-Induced Fluorescence Enhancement to Identify Stable Local Conformations One &#945;-Synuclein Monomer at a Time
07:56

Utilizing Time-Resolved Protein-Induced Fluorescence Enhancement to Identify Stable Local Conformations One α-Synuclein Monomer at a Time

Published on: May 30, 2021

3.5K
Studying Pre-formed Fibril Induced &#945;-Synuclein Accumulation in Primary Embryonic Mouse Midbrain Dopamine Neurons
10:03

Studying Pre-formed Fibril Induced α-Synuclein Accumulation in Primary Embryonic Mouse Midbrain Dopamine Neurons

Published on: August 16, 2020

11.1K
Generation of Alpha-Synuclein Preformed Fibrils from Monomers and Use In Vivo
09:44

Generation of Alpha-Synuclein Preformed Fibrils from Monomers and Use In Vivo

Published on: June 2, 2019

22.3K

Area of Science:

  • Neuroscience
  • Chemical Biology
  • Molecular Imaging

Background:

  • Alpha-synuclein (α-synuclein) aggregation is a hallmark of neurodegenerative synucleinopathies.
  • Fluorescent probes are crucial for visualizing α-synuclein pathology in vitro and in vivo.
  • Developing specific and sensitive probes remains a challenge.

Purpose of the Study:

  • To investigate benzofuranone as a scaffold for designing fluorescent probes targeting α-synuclein.
  • To evaluate the binding affinity and specificity of these novel probes to α-synuclein aggregates.
  • To assess the probes' utility in distinguishing different pathological inclusions in post-mortem brain tissue.

Main Methods:

  • Synthesis and characterization of benzofuranone-based small molecules.
  • In vitro assays to determine binding affinity to α-synuclein fibrils.
  • Fluorescence microscopy and spectroscopy to assess probe performance.
  • Application of probes to post-mortem human brain tissue with various synucleinopathies.

Main Results:

  • Benzofuranone compounds demonstrated high affinity for α-synuclein.
  • Probes exhibited a fluorescent "turn-on" response upon binding to α-synuclein fibrils.
  • Distinct binding patterns were observed for Lewy bodies, Lewy neurites, and glial cytoplasmic inclusions.
  • The probes successfully visualized α-synuclein pathology in post-mortem brain tissue.

Conclusions:

  • Benzofuranone derivatives show significant potential as specific fluorescent probes for α-synuclein.
  • These probes can differentiate between various α-synuclein aggregate types.
  • The findings suggest conformational differences in α-synucleinopathies and distinct binding sites for small molecules.