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

Amplifying Signals via Enzymatic Cascade01:22

Amplifying Signals via Enzymatic Cascade

10.3K
When a ligand binds to a cell-surface receptor, the receptor's intracellular domain changes shape, which may either activate its enzyme function or allow its binding to other molecules. The initial signal is amplified by most signal transduction pathways. This means that a single ligand molecule can activate multiple molecules of a downstream target. Proteins that relay a signal are most commonly phosphorylated at one or more sites, activating or inactivating the protein. Kinases catalyze...
10.3K
Enzyme-linked Receptors01:00

Enzyme-linked Receptors

80.2K
Enzyme-linked receptors are proteins that act as both receptor and enzyme, activating multiple intracellular signals. This is a large group of receptors that include the receptor tyrosine kinase (RTK) family. Many growth factors and hormones bind to and activate the RTKs.
Neurotrophin (NT) receptors are a family of RTKs, including trkA, trkB, and trkC (tropomyosin-related kinase) receptors. TrkA is specific for nerve growth factor (NGF), neurotrophin-6, and neurotrophin-7. TrkB binds...
80.2K
Protein Complex Assembly02:41

Protein Complex Assembly

11.6K
Proteins can form homomeric complexes with another unit of the same protein or heteromeric complexes with different types.  Most protein complexes self-assemble spontaneously via ordered pathways, while some proteins need assembly factors that guide their proper assembly. Despite the crowded intracellular environment, proteins usually interact with their correct partners and form functional complexes.
Many viruses self-assemble into a fully functional unit using the infected host cell to...
11.6K
Protein Complexes with Interchangeable Parts01:57

Protein Complexes with Interchangeable Parts

2.6K
Groups of proteins may form a complex where each protein in this complex has a different role in the overall execution of the complex’s function. Often some of the proteins in the complex can be replaced by a closely related variant to give a complex that contains many of the same components yet is functionally distinct.
The SCF ubiquitin ligase is a protein complex of five individual proteins. This complex attaches ubiquitin to other target proteins to mark them for degradation. In order...
2.6K
Transducer Mechanism: Enzyme-Linked Receptors01:27

Transducer Mechanism: Enzyme-Linked Receptors

2.9K
Enzyme-linked receptors are cell-surface receptors acting as an enzyme or associating with an enzyme intracellularly. They make excellent drug targets. Drugs can bind to the extracellular ligand-binding domain or directly affect their enzymatic domain and alter their activity.
Major types that are helpful drug targets include:
2.9K
The Supercomplexes in the Crista Membrane01:41

The Supercomplexes in the Crista Membrane

2.6K
The mitochondrial cristae membrane is the primary site for the oxidative phosphorylation (OXPHOS) process of energy conversion mediated through respiratory complexes I to V. These complexes have been widely studied for decades, and it has been proven that they form supramolecular structures called respiratory supercomplexes (SC). These higher-order complexes may be crucial in maintaining the biochemical structure and improving the physiological activity of the individual complexes while...
2.6K

You might also read

Related Articles

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

Sort by
Same author

Phosphorylated Nanocellulose/Surfactant-Stabilized Middle-Phase Microemulsions for Enhanced Oil Recovery.

Langmuir : the ACS journal of surfaces and colloids·2026
Same author

Construction of an aptamer-conjugated molecular artificial enzyme with enhanced activity and selectivity.

Organic & biomolecular chemistry·2026
Same author

Rapid fabrication of sustainable bioplastics from phosphorylated cellulose microfibers via hot-press assisted dual crosslinking with enhanced mechanical and thermal properties.

International journal of biological macromolecules·2026
Same author

Modular design of dual-targeted, enzyme-responsive peptide carriers for gene drug delivery.

Nanoscale horizons·2026
Same author

Bioinspired Long-Lived SLIPS for Synergistic Drag Reduction, Corrosion Protection, and Marine Antifouling.

Langmuir : the ACS journal of surfaces and colloids·2026
Same author

Multifunctional Bio-Based Packaging for Perishable Foods: Structural Design, Scalable Fabrication, and Versatile Applications.

Advanced materials (Deerfield Beach, Fla.)·2026

Related Experiment Video

Updated: Sep 23, 2025

Analyzing Dynamic Protein Complexes Assembled On and Released From Biolayer Interferometry Biosensor Using Mass Spectrometry and Electron Microscopy
09:30

Analyzing Dynamic Protein Complexes Assembled On and Released From Biolayer Interferometry Biosensor Using Mass Spectrometry and Electron Microscopy

Published on: August 6, 2018

9.5K

A light-responsive multienzyme complex combining cascade enzymes within a peptide-based matrix.

Yutong Wang1, Yifei Zhang1, Mengfan Wang1,2

  • 1State Key Laboratory of Chemical Engineering, School of Chemical Engineering and Technology, Tianjin University Tianjin 300072 P. R. China mwang@tju.edu.cn qiwei@tju.edu.cn.

RSC Advances
|May 11, 2022
PubMed
Summary

Researchers developed a light-responsive multienzyme complex using a peptide matrix. This advanced material enhances enzyme activity and allows light-controlled modulation for improved cascade reactions.

More Related Videos

Bioluminescent Optogenetics 2.0: Harnessing Bioluminescence to Activate Photosensory Proteins In Vitro and In Vivo
07:19

Bioluminescent Optogenetics 2.0: Harnessing Bioluminescence to Activate Photosensory Proteins In Vitro and In Vivo

Published on: August 4, 2021

4.8K
OaAEP1-Mediated Enzymatic Synthesis and Immobilization of Polymerized Protein for Single-Molecule Force Spectroscopy
08:34

OaAEP1-Mediated Enzymatic Synthesis and Immobilization of Polymerized Protein for Single-Molecule Force Spectroscopy

Published on: February 5, 2020

6.8K

Related Experiment Videos

Last Updated: Sep 23, 2025

Analyzing Dynamic Protein Complexes Assembled On and Released From Biolayer Interferometry Biosensor Using Mass Spectrometry and Electron Microscopy
09:30

Analyzing Dynamic Protein Complexes Assembled On and Released From Biolayer Interferometry Biosensor Using Mass Spectrometry and Electron Microscopy

Published on: August 6, 2018

9.5K
Bioluminescent Optogenetics 2.0: Harnessing Bioluminescence to Activate Photosensory Proteins In Vitro and In Vivo
07:19

Bioluminescent Optogenetics 2.0: Harnessing Bioluminescence to Activate Photosensory Proteins In Vitro and In Vivo

Published on: August 4, 2021

4.8K
OaAEP1-Mediated Enzymatic Synthesis and Immobilization of Polymerized Protein for Single-Molecule Force Spectroscopy
08:34

OaAEP1-Mediated Enzymatic Synthesis and Immobilization of Polymerized Protein for Single-Molecule Force Spectroscopy

Published on: February 5, 2020

6.8K

Area of Science:

  • Biomaterials Science
  • Enzyme Engineering
  • Supramolecular Chemistry

Background:

  • Multienzyme complexes offer enhanced catalytic efficiency through proximity effects and intermediate channeling.
  • Stimuli-responsive materials provide dynamic control over biological processes.
  • Peptide-based matrices offer biocompatibility and tunable structural properties.

Purpose of the Study:

  • To develop a light-responsive multienzyme complex for controlled cascade reactions.
  • To engineer a peptide-based supramolecular matrix incorporating glucose oxidase and hemin.
  • To investigate the light-modulated catalytic activity of the engineered complex.

Main Methods:

  • Incorporation of glucose oxidase (GOx) and hemin into a glycine-phenylalanine-glycine (GFG) tripeptide matrix functionalized with an azobenzene (Azo) group.
  • Utilizing the light-induced E/Z isomerization of azobenzene to modulate the peptide matrix structure.
  • Assessing the catalytic activity of the GOx&hemin@PepM complex in cascade reactions and comparing it to free enzymes.

Main Results:

  • The GOx&hemin@PepM complex exhibited significantly enhanced catalytic activity compared to free enzymes due to proximity effects and a biomimetic microenvironment.
  • The azobenzene moiety enabled light-responsive conformational switching, allowing external control over the peptide matrix structure.
  • Catalytic activity of the multienzyme complex could be precisely modulated using UV and visible light.

Conclusions:

  • A novel light-responsive multienzyme complex (GOx&hemin@PepM) was successfully constructed using an adjustable peptide-based material platform.
  • The developed system demonstrates efficient cascade reaction catalysis with externally controllable activity via light stimuli.
  • This work presents a new strategy for designing stimuli-responsive enzyme systems for advanced applications.