Search research articles

ABOUT JoVE

Overview Leadership Blog JoVE Help Center

AUTHORS

Publishing Process Editorial Board Scope & Policies Peer Review FAQ Submit

LIBRARIANS

Testimonials Subscriptions Access Resources Library Advisory Board FAQ

RESEARCH

JoVE Journal Methods Collections JoVE Encyclopedia of Experiments Archive

EDUCATION

JoVE Core JoVE Business JoVE Science Education JoVE Lab Manual Faculty Resource Center Faculty Site

Terms & Conditions of Use

Related Concept Videos

Antibody Structure

Antibody Structure

Overview
Antibodies, also known as immunoglobulins (Ig), are essential players of the adaptive immune system. These antigen-binding proteins are produced by B cells and make up 20 percent of the total blood plasma by weight. In mammals, antibodies fall into five different classes, which each elicits a different biological response upon antigen binding.
The Y-Shaped Structure of Antibodies Consists of Four Polypeptide Chains
Antibodies consist of four polypeptide chains: two identical heavy...

Antibody Structure

Antibody Structure

Overview
Antibodies, also known as immunoglobulins (Ig), are essential players of the adaptive immune system. These antigen-binding proteins are produced by B cells and make up 20 percent of the total blood plasma by weight. In mammals, antibodies fall into five different classes, which each elicits a different biological response upon antigen binding.
The Y-Shaped Structure of Antibodies Consists of Four Polypeptide Chains
Antibodies consist of four polypeptide chains: two identical heavy...

Antibody Structure and Classes

Antibody Structure and Classes

Antibodies, also known as immunoglobulins, are produced by B cells in response to foreign substances, such as bacteria and viruses. These proteins are critical for recognizing and neutralizing these substances, protecting the body from potential harm.
The basic structure of an antibody consists of four protein chains: two identical heavy chains and two identical light chains. These chains are held together by disulfide bonds and other non-covalent interactions, forming a Y-shaped structure.

Antibody Actions

Antibody Actions

Antibodies, or immunoglobulins, are critical players in the immune system's arsenal against invading pathogens. Produced by B cells and plasma cells, their primary role is to detect and bind to specific antigens, molecules found on the surface of pathogens like bacteria or viruses. Beyond antigen recognition, antibodies perform several vital functions that contribute to immune defense.
Neutralization
Antibodies can bind to pathogens, preventing them from infecting host cells. This process...

You might also read

Related Articles

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

Sort by

Same author

Chemical and biological profiling of bioactive metabolites from the invertebrate-pathogenic fungus Gibellula scorpioides BCC 39989.

Scientific reports·2026

Same author

Simultaneous targeted delivery of doxorubicin and KRAS suppression by a hybrid molecule containing miR-143 and AS1411 aptamer.

Scientific reports·2025

Same author

Multifunctional molecular hybrid for targeted colorectal cancer cells: Integrating doxorubicin, AS1411 aptamer, and T9/U4 ASO.

PloS one·2025

Same author

Anti-proliferation and induction of mitochondria-mediated apoptosis by

Heliyon·2023

Same author

Anti-Proliferative Effect of Doxorubicin-Loaded AS1411 Aptamer on Colorectal Cancer Cell.

Asian Pacific journal of cancer prevention : APJCP·2021

Same author

A molecular hybrid comprising AS1411 and PDGF-BB aptamer, cholesterol, and doxorubicin for inhibiting proliferation of SW480 cells.

Journal of molecular recognition : JMR·2021

Search research articles

Related Experiment Video

Updated: Jun 10, 2026

Folding and Characterization of a Bio-responsive Robot from DNA Origami

Folding and Characterization of a Bio-responsive Robot from DNA Origami

Published on: December 3, 2015

A temperature-responsive antibody-like nanostructure.

Jing Zhou¹, Boonchoy Soontornworajit, Yong Wang

¹Department of Chemical, Materials, and Biomolecular Engineering, University of Connecticut, Storrs, Connecticut 06269-3222, USA.

Biomacromolecules

|August 10, 2010

Summary

This summary is machine-generated.

Researchers developed a novel antibody-like nanostructure using DNA aptamers and a dendrimer. This nanostructure offers tunable binding and controlled release, overcoming limitations of natural antibodies.

More Related Videos

Ligand Nano-cluster Arrays in a Supported Lipid Bilayer

Ligand Nano-cluster Arrays in a Supported Lipid Bilayer

Published on: April 23, 2017

Synthesis of Immunotargeted Magneto-plasmonic Nanoclusters

Synthesis of Immunotargeted Magneto-plasmonic Nanoclusters

Published on: August 22, 2014

Related Experiment Videos

Last Updated: Jun 10, 2026

Folding and Characterization of a Bio-responsive Robot from DNA Origami

Folding and Characterization of a Bio-responsive Robot from DNA Origami

Published on: December 3, 2015

Ligand Nano-cluster Arrays in a Supported Lipid Bilayer

Ligand Nano-cluster Arrays in a Supported Lipid Bilayer

Published on: April 23, 2017

Synthesis of Immunotargeted Magneto-plasmonic Nanoclusters

Synthesis of Immunotargeted Magneto-plasmonic Nanoclusters

Published on: August 22, 2014

Area of Science:

Biotechnology
Nanotechnology
Molecular Biology

Background:

Antibodies are crucial in various applications but face challenges with tunable binding and chemical conjugation.
Natural antibodies have limitations in nonphysiological conditions and controlled dissociation.

Purpose of the Study:

To develop a novel antibody-like nanostructure with tunable binding and controlled release capabilities.
To overcome the limitations of natural antibodies in specific applications.

Main Methods:

Constructed a bivalent nanostructure using two DNA aptamers and a dendrimer.
DNA aptamers mimicked antigen-binding sites, while the dendrimer provided a conjugation site.
Investigated binding affinity, specificity, and temperature-triggered dissociation.

Main Results:

The bivalent nanostructure demonstrated high binding affinity and specificity for target cells.
A temperature shift from 0 to 37°C induced rapid dissociation from bound target cells.
This controlled dissociation is a feature not found in natural antibody-antigen complexes.

Conclusions:

Successfully developed an antibody-like nanostructure with unique, tunable features.
The nanostructure offers advantages over natural antibodies for applications requiring controlled binding and release.
This innovation has potential applications in diagnostics, therapeutics, and biomaterials.