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

Sensors without Borders.

ACS sensors·2026
Same author

Engineering a Transmembrane Receptor for Coacervate-Based Artificial Cells.

Journal of the American Chemical Society·2026
Same author

Thermostable Bioluminescent Intercalating Dyes for Real-Time, Integrated Nucleic Acid Amplification and Detection.

Angewandte Chemie (International ed. in English)·2026
Same author

Homogeneous Antibody-DNA Conjugates Using Unmodified Oligonucleotides and Photo-Cross-Linkable Protein G-HUH Endonuclease Fusion Proteins.

Bioconjugate chemistry·2026
Same author

Restoring the 14-3-3/CRAF regulatory interaction in Noonan syndrome using molecular glues.

Proceedings of the National Academy of Sciences of the United States of America·2026
Same author

Multicolor Bioluminescent Toolbox for Multiplex Glow-in-the-Dark Nucleic Acid Diagnostics.

ACS sensors·2026

Related Experiment Video

Updated: Mar 18, 2026

Demonstration of Heterologous Complexes formed by Golgi-Resident Type III Membrane Proteins using Split Luciferase Complementation Assay
05:28

Demonstration of Heterologous Complexes formed by Golgi-Resident Type III Membrane Proteins using Split Luciferase Complementation Assay

Published on: September 10, 2020

2.8K

Supramolecular Control over Split-Luciferase Complementation.

Ralph P G Bosmans1, Jeroen M Briels1, Lech-Gustav Milroy1

  • 1Laboratory of Chemical Biology and Institute of Complex Molecular Systems, Department of Biomedical Engineering, Eindhoven University of Technology, Den Dolech 2, 5612, AZ, Eindhoven, The Netherlands.

Angewandte Chemie (International Ed. in English)
|June 30, 2016
PubMed
Summary
This summary is machine-generated.

Researchers developed a novel supramolecular system using split-luciferase and cucurbit[8]uril (Q8) to control enzyme activity. This host-guest interaction enables reversible on-off switching of luciferase, offering a versatile tool for molecular signaling.

Keywords:
cooperativitycucurbit[8]urilsplit-luciferasesupramolecular chemical biologyswitching

More Related Videos

Luciferase Complementation Imaging Assay in Nicotiana benthamiana Leaves for Transiently Determining Protein-protein Interaction Dynamics
07:55

Luciferase Complementation Imaging Assay in Nicotiana benthamiana Leaves for Transiently Determining Protein-protein Interaction Dynamics

Published on: November 20, 2017

15.0K
Author Spotlight: Regulation and Dysregulation of ER-Mitochondria Contacts — Implications for Neurodegenerative Disease Pathogenesis
09:09

Author Spotlight: Regulation and Dysregulation of ER-Mitochondria Contacts — Implications for Neurodegenerative Disease Pathogenesis

Published on: October 11, 2024

3.1K

Related Experiment Videos

Last Updated: Mar 18, 2026

Demonstration of Heterologous Complexes formed by Golgi-Resident Type III Membrane Proteins using Split Luciferase Complementation Assay
05:28

Demonstration of Heterologous Complexes formed by Golgi-Resident Type III Membrane Proteins using Split Luciferase Complementation Assay

Published on: September 10, 2020

2.8K
Luciferase Complementation Imaging Assay in Nicotiana benthamiana Leaves for Transiently Determining Protein-protein Interaction Dynamics
07:55

Luciferase Complementation Imaging Assay in Nicotiana benthamiana Leaves for Transiently Determining Protein-protein Interaction Dynamics

Published on: November 20, 2017

15.0K
Author Spotlight: Regulation and Dysregulation of ER-Mitochondria Contacts — Implications for Neurodegenerative Disease Pathogenesis
09:09

Author Spotlight: Regulation and Dysregulation of ER-Mitochondria Contacts — Implications for Neurodegenerative Disease Pathogenesis

Published on: October 11, 2024

3.1K

Area of Science:

  • Supramolecular Chemistry
  • Biochemistry
  • Molecular Biology

Background:

  • Split-enzyme complementation is a powerful technique for reconstituting protein function.
  • Controlling enzyme activity with external stimuli is crucial for developing responsive molecular systems.
  • Host-guest chemistry offers precise molecular recognition for assembling supramolecular complexes.

Purpose of the Study:

  • To engineer a supramolecular system for reversible on-off switching of enzymatic activity.
  • To utilize host-guest binding between cucurbit[8]uril (Q8) and modified split-luciferase fragments.
  • To establish a controllable module for in vitro supramolecular signaling networks.

Main Methods:

  • Designing split-luciferase fragments with an N-terminal FGG sequence for Q8 binding.
  • Screening for complementation driven by Q8-mediated host-guest interactions.
  • Investigating the reversibility of complementation using Q8 inhibitors and competition studies.

Main Results:

  • Achieved a 20-fold upregulation of luciferase activity through Q8-induced supramolecular complementation.
  • Demonstrated full reversibility of enzyme activity using Q8 inhibitors.
  • Observed a 300-fold enhanced stability of the ternary heterocomplex compared to fragment self-binding.

Conclusions:

  • Supramolecular split-enzyme complementation provides a robust method for controlling enzymatic activity.
  • The Q8-luciferase system offers reversible on-off switching, suitable for molecular signaling.
  • This approach yields a versatile module for constructing dynamic supramolecular systems.