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

Ligand Binding Sites02:40

Ligand Binding Sites

15.2K
Proteins are dynamic macromolecules that carry out a wide variety of essential processes; however, the activities of most proteins depend on their interactions with other molecules or ions, known as ligands.
Protein-ligand interactions are quite specific; even though numerous potential ligands surround a cellular protein at any given time, only a particular ligand can bind to that protein. Moreover, a ligand binds only to a dedicated area on the surface of the protein, known as the...
15.2K
Ligand Binding Sites02:40

Ligand Binding Sites

8.9K
8.9K
Conserved Binding Sites01:49

Conserved Binding Sites

5.2K
Many proteins’ biological role depends on their interactions with their ligands, small molecules that bind to specific locations on the protein known as ligand-binding sites. Ligand-binding sites are often conserved among homologous proteins as these sites are critical for protein function.
Binding sites are often located in large pockets, and if their location on a protein’s surface is unknown, it can be predicted using various approaches. The energetic method computationally...
5.2K
Conserved Binding Sites01:49

Conserved Binding Sites

2.0K
2.0K
Amyloid Fibrils03:03

Amyloid Fibrils

12.0K
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,...
12.0K
Amyloid Fibrils03:03

Amyloid Fibrils

6.5K
6.5K

You might also read

Related Articles

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

Sort by
Same author

The spectrum of heart failure: prevalence and years lived with disability of heart failure across 2 severity levels and implications for health systems: a population-based comparative study.

European journal of cardiovascular nursing·2026
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

Automated scoliosis X-ray cobb angle classification: a deep learning approach with RadImageNet.

European spine journal : official publication of the European Spine Society, the European Spinal Deformity Society, and the European Section of the Cervical Spine Research Society·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

Podcasts as Digital Scholarship in Surgical Education and Professional Development: Perspectives from Learners to Leaders.

Annals of surgery·2026

Related Experiment Video

Updated: Feb 10, 2026

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

22.6K

Alpha Synuclein Fibrils Contain Multiple Binding Sites for Small Molecules.

Chia-Ju Hsieh1, John J Ferrie2, Kuiying Xu1

  • 1Department of Radiology, Perelman School of Medicine , University of Pennsylvania , Philadelphia , Pennsylvania 19104 , United States.

ACS Chemical Neuroscience
|May 12, 2018
PubMed
Summary

Researchers identified three binding sites on alpha synuclein (Asyn) fibrils, crucial for Parkinson's disease imaging. This knowledge aids in designing probes to detect Asyn protein aggregates.

Keywords:
Alpha synucleinLewy bodiesLewy neuritesParkinson’s disease

More Related Videos

Bioluminescence Imaging of Neuroinflammation in Transgenic Mice After Peripheral Inoculation of Alpha-Synuclein Fibrils
09:32

Bioluminescence Imaging of Neuroinflammation in Transgenic Mice After Peripheral Inoculation of Alpha-Synuclein Fibrils

Published on: April 13, 2017

9.0K
Exogenous Administration of Microsomes-associated Alpha-synuclein Aggregates to Primary Neurons As a Powerful Cell Model of Fibrils Formation
09:16

Exogenous Administration of Microsomes-associated Alpha-synuclein Aggregates to Primary Neurons As a Powerful Cell Model of Fibrils Formation

Published on: June 26, 2018

8.0K

Related Experiment Videos

Last Updated: Feb 10, 2026

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

22.6K
Bioluminescence Imaging of Neuroinflammation in Transgenic Mice After Peripheral Inoculation of Alpha-Synuclein Fibrils
09:32

Bioluminescence Imaging of Neuroinflammation in Transgenic Mice After Peripheral Inoculation of Alpha-Synuclein Fibrils

Published on: April 13, 2017

9.0K
Exogenous Administration of Microsomes-associated Alpha-synuclein Aggregates to Primary Neurons As a Powerful Cell Model of Fibrils Formation
09:16

Exogenous Administration of Microsomes-associated Alpha-synuclein Aggregates to Primary Neurons As a Powerful Cell Model of Fibrils Formation

Published on: June 26, 2018

8.0K

Area of Science:

  • Neuroscience
  • Biochemistry
  • Molecular Biology

Background:

  • Fibrillary aggregation of alpha synuclein (Asyn) is a key pathological hallmark of Parkinson's disease (PD).
  • Developing diagnostic imaging probes for Asyn fibrils is critical for early PD detection and monitoring.

Purpose of the Study:

  • To identify and characterize small molecule binding sites on Asyn fibrils.
  • To provide a foundation for designing high-affinity imaging probes for fibrillar Asyn species.

Main Methods:

  • Employed a combination of molecular modeling, photoaffinity labeling, and mass spectrometry.
  • Utilized radioligand binding studies to assess molecule affinity for Asyn fibrils.

Main Results:

  • Discovered three distinct binding sites within fibrillar Asyn.
  • These sites demonstrated moderate to high affinity for small molecule ligands.
  • Identified specific amino acid residues constituting these binding pockets.

Conclusions:

  • The identified binding sites are suitable targets for small molecule interaction.
  • Understanding these residues is essential for the rational design of novel diagnostic probes for Parkinson's disease.