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

You might also read

Related Articles

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

Sort by
Same author

Discovery of CNS Penetrant SOS1 Inhibitors for the Treatment of KRAS-Dependent Cancers.

Journal of medicinal chemistry·2026
Same author

Molecular Basis of c‑MET Inhibition by Approved Small Molecule Drugs: A Structural Perspective.

ACS medicinal chemistry letters·2026
Same author

Discovery and Characterization of Diverse Non-nucleotide Inhibitors of DNPH1 Using an Integrated Hit Finding Strategy.

ACS medicinal chemistry letters·2026
Same author

Discovery and Optimization of a Non-Nucleoside-Based Series of Inhibitors of 2'-Deoxynucleoside 5'-Monophosphate Glycosidase (DNPH1).

Journal of medicinal chemistry·2025
Same author

Use of Direct-to-Biology Strategies for the Discovery of 2'-Deoxynucleoside 5'-Monophosphate N-Glycosidase (DNPH1) PROTACs.

Journal of medicinal chemistry·2025
Same author

High-density Phenotype Data of Intermediate Phenotypes Associated with Stalk Lodging Resistance in Maize.

Scientific data·2025

Related Experiment Video

Updated: May 21, 2026

High Sensitivity Measurement of Transcription Factor-DNA Binding Affinities by Competitive Titration Using Fluorescence Microscopy
06:38

High Sensitivity Measurement of Transcription Factor-DNA Binding Affinities by Competitive Titration Using Fluorescence Microscopy

Published on: February 7, 2019

High-throughput interrogation of ligand binding mode using a fluorescence-based assay.

Paweł Śledź1, Steffen Lang, Christopher J Stubbs

  • 1University Chemical Laboratory, University of Cambridge, Lensfield Road, Cambridge CB2 1EW, UK.

Angewandte Chemie (International Ed. in English)
|June 26, 2012
PubMed
Summary

A novel fluorescence-based thermal shift assay rapidly evaluates how different protein forms bind to ligands. This method aids in understanding structure-activity relationships for Plk1, a key target in anticancer drug development.

More Related Videos

A "Dual-Addition" Calcium Fluorescence Assay for the High-Throughput Screening of Recombinant G Protein-Coupled Receptors
08:46

A "Dual-Addition" Calcium Fluorescence Assay for the High-Throughput Screening of Recombinant G Protein-Coupled Receptors

Published on: December 2, 2022

A Fluorescence-based Lymphocyte Assay Suitable for High-throughput Screening of Small Molecules
08:43

A Fluorescence-based Lymphocyte Assay Suitable for High-throughput Screening of Small Molecules

Published on: March 10, 2017

Related Experiment Videos

Last Updated: May 21, 2026

High Sensitivity Measurement of Transcription Factor-DNA Binding Affinities by Competitive Titration Using Fluorescence Microscopy
06:38

High Sensitivity Measurement of Transcription Factor-DNA Binding Affinities by Competitive Titration Using Fluorescence Microscopy

Published on: February 7, 2019

A "Dual-Addition" Calcium Fluorescence Assay for the High-Throughput Screening of Recombinant G Protein-Coupled Receptors
08:46

A "Dual-Addition" Calcium Fluorescence Assay for the High-Throughput Screening of Recombinant G Protein-Coupled Receptors

Published on: December 2, 2022

A Fluorescence-based Lymphocyte Assay Suitable for High-throughput Screening of Small Molecules
08:43

A Fluorescence-based Lymphocyte Assay Suitable for High-throughput Screening of Small Molecules

Published on: March 10, 2017

Area of Science:

  • Biochemistry
  • Structural Biology
  • Pharmacology

Background:

  • Polo-like kinase 1 (Plk1) is a critical target in anticancer therapy.
  • Understanding ligand-protein interactions is crucial for developing effective anticancer drugs.
  • Structure-activity relationship (SAR) studies are essential for drug discovery.

Purpose of the Study:

  • To develop and validate a high-throughput fluorescence-based thermal shift (FTS) assay.
  • To establish the binding mode of ligands to Plk1.
  • To enable rapid evaluation of SAR for Plk1 ligands.

Main Methods:

  • Utilized a high-throughput fluorescence-based thermal shift (FTS) assay.
  • Employed different forms of the target protein.
  • Analyzed protein-ligand interactions to determine binding modes.

Main Results:

  • Successfully established the binding mode of ligands to the protein.
  • Demonstrated the assay's utility in rapid SAR evaluation.
  • Validated the FTS assay for probing protein-ligand interactions.

Conclusions:

  • The developed FTS assay is effective for rapid assessment of ligand binding modes.
  • This method accelerates the evaluation of structure-activity binding-mode relationships.
  • The assay provides a valuable tool for anticancer drug discovery targeting Plk1.