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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
Antibodies consist of four polypeptide chains: two identical heavy...
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Antibody Structure01:10

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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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Protein Organization01:24

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Proteins are polymers of amino acid residues. They are versatile and responsible for different cellular functions, including DNA replication, molecular transport, catalysis, and structural support. Proteins have a hierarchical structure comprising at least three levels of organization: primary, secondary, and tertiary structure. Some large proteins have a quaternary structure where individual protein subunits are linked together.
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Protein WISDOM: A Workbench for In silico De novo Design of BioMolecules
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Antibody humanization by structure-based computational protein design.

Yoonjoo Choi1, Casey Hua2,3, Charles L Sentman3

  • 1a Department of Computer Science ; Dartmouth College ; Hanover , NH USA.

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|August 8, 2015
PubMed
Summary
This summary is machine-generated.

A new method, Computationally-Driven Antibody Humanization (CoDAH), uses computational protein design to create humanized antibodies. This approach successfully generated functional humanized antibodies with high antigen binding affinity, outperforming traditional methods.

Keywords:
antibodycomputational protein designhuman string contenthumanizationpareto optimizationprotein structure analysis

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Area of Science:

  • Immunology
  • Protein Engineering
  • Computational Biology

Background:

  • Therapeutic antibodies from non-human sources require modification to reduce immune responses.
  • Traditional complementarity-determining region (CDR) grafting for antibody humanization can compromise stability and antigen binding affinity.

Purpose of the Study:

  • To introduce Computationally-Driven Antibody Humanization (CoDAH), an alternative method for antibody humanization.
  • To assess CoDAH's ability to enhance antibody humanness while preserving structural stability and antigen binding.
  • To demonstrate CoDAH's efficacy in generating functional humanized antibodies.

Main Methods:

  • CoDAH utilizes computational protein design to select amino acids from human germline sequences for antibody humanization.
  • Retrospective analyses evaluated CoDAH's effectiveness in identifying beneficial variants based on humanness and stability.
  • Prospective application involved designing and producing humanized variants of a murine anti-B7H6 antibody (TZ47).

Main Results:

  • CoDAH identified beneficial variants for humanness and structural stability, even without crystal structures.
  • 75% of computationally designed humanized antibody variants (6 of 8) were successfully expressed and bound to the B7H6 antigen.
  • Four variants exhibited binding affinity (KD) within an order of magnitude of the original murine antibody.
  • A traditional CDR-grafted variant failed to express, highlighting CoDAH's advantage.

Conclusions:

  • CoDAH offers an efficient computational approach for generating functional humanized antibodies.
  • The method successfully maintains antigen binding affinity and structural stability during humanization.
  • CoDAH provides viable humanized antibody templates for subsequent affinity maturation.