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

Protein Complexes with Interchangeable Parts01:57

Protein Complexes with Interchangeable Parts

3.0K
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...
3.0K
Enzyme-linked Receptors01:00

Enzyme-linked Receptors

88.4K
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...
88.4K

You might also read

Related Articles

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

Sort by
Same author

Rising dust pollution across Europe in a changing climate.

Nature·2026
Same author

Microporous Polyamine (PIM-EA-TB) Modified with Hydrated NiMoO<sub>4</sub> Enhances the Photocatalytic Reduction of Nitrogen to Ammonia.

ACS applied engineering materials·2026
Same author

NAP: an open source pipeline for cross-domain microbiome profiling using Nanopore sequencing-derived amplicon data.

BMC bioinformatics·2026
Same author

High-speed atomic force microscopy of membrane and membrane protein dynamics.

Current opinion in structural biology·2026
Same author

Chemiluminescence Detection of Hydrogen Peroxide with a Polymer of an Intrinsic Microporosity Solid State Emitter.

ACS applied polymer materials·2026
Same author

A Machine Learning Approach to Understand Thermal Desorption Profiles of Levoglucosan from FIGAERO-CIMS.

Environmental science & technology·2026

Related Experiment Video

Updated: Mar 17, 2026

GENPLAT: an Automated Platform for Biomass Enzyme Discovery and Cocktail Optimization
11:38

GENPLAT: an Automated Platform for Biomass Enzyme Discovery and Cocktail Optimization

Published on: October 24, 2011

16.0K

A Modular Bioplatform Based on a Versatile Supramolecular Multienzyme Complex Directly Attached to Graphene.

Abeer Alshammari1, Mareike G Posner, Abhishek Upadhyay

  • 1Department of Physics, King Saud University , Riyadh 11451, Saudi Arabia.

ACS Applied Materials & Interfaces
|July 23, 2016
PubMed
Summary

Researchers developed a modular bioplatform using supramolecular enzyme complexes on graphene. This adaptable graphene-based platform immobilizes enzymes without function loss, enabling versatile applications.

Keywords:
E2 complexesbiosensingfunctional hybrid interfacesgraphenesupramolecular dihydrolipoyl acyltransferase complexes

More Related Videos

Bridging the Bio-Electronic Interface with Biofabrication
16:38

Bridging the Bio-Electronic Interface with Biofabrication

Published on: June 6, 2012

17.4K
Multi-enzyme Screening Using a High-throughput Genetic Enzyme Screening System
08:10

Multi-enzyme Screening Using a High-throughput Genetic Enzyme Screening System

Published on: August 8, 2016

9.4K

Related Experiment Videos

Last Updated: Mar 17, 2026

GENPLAT: an Automated Platform for Biomass Enzyme Discovery and Cocktail Optimization
11:38

GENPLAT: an Automated Platform for Biomass Enzyme Discovery and Cocktail Optimization

Published on: October 24, 2011

16.0K
Bridging the Bio-Electronic Interface with Biofabrication
16:38

Bridging the Bio-Electronic Interface with Biofabrication

Published on: June 6, 2012

17.4K
Multi-enzyme Screening Using a High-throughput Genetic Enzyme Screening System
08:10

Multi-enzyme Screening Using a High-throughput Genetic Enzyme Screening System

Published on: August 8, 2016

9.4K

Area of Science:

  • Biotechnology
  • Materials Science
  • Enzyme Engineering

Background:

  • Developing adaptable bioplatforms is difficult due to protein immobilization challenges and the need for specific component combinations.
  • Protein immobilization often leads to reduced protein function, hindering the creation of effective multifunctional surfaces.

Purpose of the Study:

  • To introduce a generic, modular strategy for constructing adaptable and multifunctional bioplatforms.
  • To demonstrate the utility of supramolecular multienzyme complexes as building blocks for bioplatforms.

Main Methods:

  • Utilized cage-like supramolecular multienzyme complexes (Thermoplasma acidophilum dihydrolipoyl acyltransferase, E2) as adaptable building blocks.
  • Immobilized E2 complexes directly and noncovalently onto graphene surfaces.
  • Engineered multifunctionality by binding partner enzymes (E1) to the E2-graphene platform.

Main Results:

  • E2 complexes formed stable monolayers on graphene, preserving supramolecular structure and molecular recognition capabilities.
  • Immobilized enzymes (E1) retained their function, with significant catalytic activity detected over a wide substrate concentration range.
  • Demonstrated multiplexing capability via patterned cotransfer of modified E2 complexes.

Conclusions:

  • The E2-graphene system provides a robust and customizable platform for creating adaptable, multifunctional biodevices.
  • This modular approach overcomes key limitations in protein immobilization and enables versatile bioplatform engineering.