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

Enzyme-Linked Immunosorbent Assay01:33

Enzyme-Linked Immunosorbent Assay

19.0K
In 1971, Peter Perlman and Eva Engvall developed an Enzyme-linked immunosorbent assay (ELISA or EIA). ELISA differs from western blot in that the assays are conducted in microtiter plates or in vivo rather than on an absorbent membrane.
There are many different types of ELISAs, but they all involve an antibody molecule whose constant region binds an enzyme, leaving the variable region free to bind its specific antigen.  Enzyme-substrate reaction allows the antigen to be visualized or...
19.0K
Transducer Mechanism: Enzyme-Linked Receptors01:27

Transducer Mechanism: Enzyme-Linked Receptors

5.0K
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:
5.0K

You might also read

Related Articles

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

Sort by
Same author

Structural basis of kinesin-1 autoinhibition and its control of microtubule-based motility.

Science advances·2026
Same author

Searching for BBB permeable phytochemical inhibitors for targeting brain cancer associated HER2 protein through free energy calculations and pharmacokinetic analysis.

Scientific reports·2026
Same author

Corrigendum to <'Co-localization and co-expression of Olfml3 with Iba1 in brain of mice'> <[Journal of Neuroimmunology, 394 (2024) 1-12/578411]>.

Journal of neuroimmunology·2026
Same author

Polypharmacy's paradox: accelerated decline in a rare case of Lafora body disease.

Postepy psychiatrii neurologii·2026
Same author

Toward Intelligent Sensing Systems: Non-Equilibrium Materials as Platforms for AI-Enabled Autonomous Discovery.

Sensors (Basel, Switzerland)·2026
Same author

Comparison of Clinical and Electrophysiological Outcomes of Local Versus Intramuscular Steroid in Mild-to-Moderate Carpal Tunnel Syndrome: An Open-Label, Blinded Endpoint Randomized Clinical Trial.

Hand (New York, N.Y.)·2026

Related Experiment Video

Updated: Apr 11, 2026

Using Extraordinary Optical Transmission to Quantify Cardiac Biomarkers in Human Serum
09:23

Using Extraordinary Optical Transmission to Quantify Cardiac Biomarkers in Human Serum

Published on: December 13, 2017

6.8K

Studies on an on/off-switchable immunosensor for troponin T.

Md Ashaduzzaman1, Aswathi Anto Antony2, N Arul Murugan3

  • 1Biosensors and Bioelectronics Centre, Department of Physics, Chemistry and Biology (IFM), Linköping University, Linköping 581 83, Sweden; Department of Applied Chemistry and Chemical Engineering, University of Dhaka, Dhaka 1000, Bangladesh.

Biosensors & Bioelectronics
|June 10, 2015
PubMed
Summary

This study introduces a smart immunosensor using temperature-responsive N-isopropylacrylamide (PNIPAAm) to control cardiac troponin T (cTnT) detection. The material enables on/off switching and regeneration, improving immunosensor design.

Keywords:
On/off-switchingProgrammable bioelectronicsSmart immunosensorsTroponin T

More Related Videos

A Sensitive and Specific Quantitation Method for Determination of Serum Cardiac Myosin Binding Protein-C by Electrochemiluminescence Immunoassay
10:12

A Sensitive and Specific Quantitation Method for Determination of Serum Cardiac Myosin Binding Protein-C by Electrochemiluminescence Immunoassay

Published on: August 8, 2013

17.2K
Fully Automated Centrifugal Microfluidic Device for Ultrasensitive Protein Detection from Whole Blood
08:58

Fully Automated Centrifugal Microfluidic Device for Ultrasensitive Protein Detection from Whole Blood

Published on: April 16, 2016

11.1K

Related Experiment Videos

Last Updated: Apr 11, 2026

Using Extraordinary Optical Transmission to Quantify Cardiac Biomarkers in Human Serum
09:23

Using Extraordinary Optical Transmission to Quantify Cardiac Biomarkers in Human Serum

Published on: December 13, 2017

6.8K
A Sensitive and Specific Quantitation Method for Determination of Serum Cardiac Myosin Binding Protein-C by Electrochemiluminescence Immunoassay
10:12

A Sensitive and Specific Quantitation Method for Determination of Serum Cardiac Myosin Binding Protein-C by Electrochemiluminescence Immunoassay

Published on: August 8, 2013

17.2K
Fully Automated Centrifugal Microfluidic Device for Ultrasensitive Protein Detection from Whole Blood
08:58

Fully Automated Centrifugal Microfluidic Device for Ultrasensitive Protein Detection from Whole Blood

Published on: April 16, 2016

11.1K

Area of Science:

  • Biomedical Engineering
  • Materials Science
  • Immunotechnology

Background:

  • Regeneration is crucial for developing effective immunosensors.
  • Current immunosensor designs often lack efficient regeneration capabilities.
  • Stimuli-responsive materials offer potential for advanced immunosensor functionalities.

Purpose of the Study:

  • To investigate the temperature-regulated interaction of N-isopropylacrylamide (PNIPAAm) functionalized cardiac troponin T (cTnT) with anti-cTnT for immunosensor applications.
  • To demonstrate the on/off-switchability and regeneration capacity of PNIPAAm-functionalized bioelectrodes.
  • To explore the role of PNIPAAm's lower critical solution temperature (LCST) in analyte recognition.

Main Methods:

  • Covalent bonding of PNIPAAm onto an anti-cTnT bioelectrode.
  • Characterization of PNIPAAm-functionalized bioelectrode performance at different temperatures.
  • Computational studies to analyze structural changes and binding free energies.
  • Measurement of antigen-antibody complex stability and interaction.

Main Results:

  • PNIPAAm functionalization enabled on/off-switchability and regeneration of the anti-cTnT bioelectrode.
  • Temperature control above the LCST created a lipophilic microenvironment facilitating cTnT binding.
  • Computational analysis revealed significant differences in free energy (ΔG) for cTnT binding at 25 °C and 37 °C.
  • Demonstrated temperature-triggered sensitivity and specific analyte recognition.

Conclusions:

  • PNIPAAm-based bioelectrodes offer a promising platform for regenerable and temperature-controlled immunosensing.
  • The temperature-responsive nature of PNIPAAm allows for programmable antigen-antibody interactions.
  • This approach paves the way for miniaturized, smart immuno-technologies with stimuli-responsive capabilities.