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Related Concept Videos

Antibody Structure01:10

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...
Protein Complex Assembly02:41

Protein Complex Assembly

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...
Antibody Structure01:10

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...
Protein-protein Interfaces02:04

Protein-protein Interfaces

Many proteins form complexes to carry out their functions, making protein-protein interactions (PPIs) essential for an organism's survival. Most PPIs are stabilized by numerous weak noncovalent chemical forces. The physical shape of the interfaces determines the way two proteins interact. Many globular proteins have closely-matching shapes on their surfaces, which form a large number of weak bonds. Additionally, many PPIs occur between two helices or between a surface cleft and a polypeptide...
Protein Complexes with Interchangeable Parts01:57

Protein Complexes with Interchangeable Parts

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 to...
Protein Complexes with Interchangeable Parts01:57

Protein Complexes with Interchangeable Parts

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 to...

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Related Experiment Video

Updated: Jun 23, 2026

Orthogonal Protein Purification Facilitated by a Small Bispecific Affinity Tag
10:32

Orthogonal Protein Purification Facilitated by a Small Bispecific Affinity Tag

Published on: January 16, 2012

Modular Platform for Efficient Assembly of Multifunctional Antibodies Using Orthogonal Protein-Protein Interactions.

Baizhen Gao1, Rushant Sabnis1, Siddhi Kotnis1

  • 1Department of Chemical Engineering, Texas A&M University, College Station, Texas 77840, United States.

ACS Applied Materials & Interfaces
|March 31, 2025
PubMed
Summary

Researchers developed a novel modular platform for creating multifunctional antibodies. This system uses specific protein interactions and elastin-like polypeptides for efficient assembly and purification, enabling diverse therapeutic applications.

Keywords:
antibody engineeringelastin-like polypeptide (ELP)nanobodyprotein purificationprotein−protein interaction

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Creating Highly Specific Chemically Induced Protein Dimerization Systems by Stepwise Phage Selection of a Combinatorial Single-Domain Antibody Library
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Creating Highly Specific Chemically Induced Protein Dimerization Systems by Stepwise Phage Selection of a Combinatorial Single-Domain Antibody Library

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Last Updated: Jun 23, 2026

Orthogonal Protein Purification Facilitated by a Small Bispecific Affinity Tag
10:32

Orthogonal Protein Purification Facilitated by a Small Bispecific Affinity Tag

Published on: January 16, 2012

Bacterial Inner-membrane Display for Screening a Library of Antibody Fragments
12:28

Bacterial Inner-membrane Display for Screening a Library of Antibody Fragments

Published on: October 15, 2016

Creating Highly Specific Chemically Induced Protein Dimerization Systems by Stepwise Phage Selection of a Combinatorial Single-Domain Antibody Library
10:17

Creating Highly Specific Chemically Induced Protein Dimerization Systems by Stepwise Phage Selection of a Combinatorial Single-Domain Antibody Library

Published on: January 14, 2020

Area of Science:

  • Biotechnology
  • Immunology
  • Protein Engineering

Background:

  • Multifunctional antibodies, engaging multiple targets simultaneously, are of increasing interest.
  • Existing methods for producing multifunctional antibodies face challenges like low yield, complex design, and difficult manufacturing.

Purpose of the Study:

  • To introduce a novel modular post-translational platform for assembling multifunctional antibodies.
  • To overcome limitations of current antibody production methods, improving yield, design, and manufacturing.

Main Methods:

  • Utilized a modular platform based on highly specific protein-protein interactions for antibody assembly.
  • Incorporated an elastin-like polypeptide (ELP) tag for simplified purification processes.
  • Demonstrated assembly of multifunctional antibodies with diverse biological functions.

Main Results:

  • Achieved over 90% assembled scaffold and high overall product purity for multifunctional antibodies.
  • Successfully generated antibodies for various applications: cancer detection, growth inhibition, and T-cell-mediated cancer cell targeting.
  • The platform demonstrated high assembly efficiency, straightforward purification, and modularity.

Conclusions:

  • The developed platform provides an efficient and modular approach for producing high-purity multifunctional antibodies.
  • This method simplifies the manufacturing process and allows for versatile redesign of antibody functions.
  • The platform holds significant potential for advancing antibody-based therapeutics and diagnostics.