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Related Concept Videos

Antibody Structure01:10

Antibody Structure

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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
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Antibody Structure and Classes01:25

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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.
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Organisms are capable of detecting and fixing nucleotide mismatches that occur during DNA replication. This sophisticated process requires identifying the new strand and replacing the erroneous bases with correct nucleotides. Mismatch repair is coordinated by many proteins in both prokaryotes and eukaryotes.
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Related Experiment Video

Updated: Sep 15, 2025

Protein Engineering by Yeast Surface Display
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Tuning antibody stability and function by rational designs of framework mutations.

Joseph C F Ng1,2,3, Alicia Chenoweth4,5, Maria Laura De Sciscio1,2,6

  • 1Research Department of Structural and Molecular Biology, Division of Biosciences, University College London, London, UK.

Mabs
|July 14, 2025
PubMed
Summary
This summary is machine-generated.

This study introduces a computational method to engineer antibody framework (FW) mutations, enhancing stability and function beyond the complementarity-determining region (CDR). The approach optimizes antibody developability by considering the entire antibody structure.

Keywords:
Antibody effector functionsAntibody engineeringAntibody frameworkAntibody language modelsAntibody stabilityArtificial intelligence

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Laboratory Scale Production and Purification of a Therapeutic Antibody
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Laboratory Scale Production and Purification of a Therapeutic Antibody

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Area of Science:

  • Biotechnology
  • Immunology
  • Computational Biology

Background:

  • Antibody engineering often focuses on complementarity-determining regions (CDRs), neglecting the immunoglobulin framework (FW).
  • The FW provides structural support crucial for antibody stability and function.
  • Existing artificial intelligence models may overlook FW contributions in antibody design.

Purpose of the Study:

  • To develop an integrated computational-experimental workflow for rational design of FW mutations.
  • To modulate antibody stability and activity by targeting the FW.
  • To expand antibody engineering strategies beyond CDR-centric approaches.

Main Methods:

  • Integrated computational-experimental workflow combining static structure analysis, molecular dynamics simulations, and in vitro assays.
  • Analysis of antibody-specific language models for insights into FW mutagenesis.
  • Design and validation of FW mutations using trastuzumab as a model antibody targeting HER2.

Main Results:

  • Computational approaches using structural information outperformed language models in predicting FW mutagenesis.
  • Designed stabilizing FW mutants distal to CDRs maintained antigen binding (HER2) and antibody-dependent cellular cytotoxicity.
  • A specific FW mutation retained antigen binding but abolished effector functions, highlighting FW's role in distal immunological functions.

Conclusions:

  • The developed workflow enables rational design of FW mutations to enhance antibody stability and function.
  • Considering the entire antibody structure, including interdomain dynamics, is crucial for optimizing antibody developability.
  • This approach expands antibody engineering scope beyond CDRs, emphasizing a holistic perspective for improved therapeutic antibodies.