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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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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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Antibody Actions01:26

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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
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Antibody Aggregation: Insights from Sequence and Structure.

Wei Li1, Ponraj Prabakaran2, Weizao Chen3

  • 1Protein Interactions Section, Cancer and Inflammation Program, Center for Cancer Research, National Cancer Institute, National Institutes of Health, Frederick, MD 21702, USA. wei.li3@nih.gov.

Antibodies (Basel, Switzerland)
|September 28, 2019
PubMed
Summary
This summary is machine-generated.

Monoclonal antibodies (mAbs) are vital biologics, but aggregation hinders development. This review links antibody structure and sequence to aggregation, offering strategies to improve therapeutic developability.

Keywords:
antibody aggregationantibody domainsantibody drug conjugatesmonoclonal antibodiesprotein unfolding

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Area of Science:

  • Biologics and biopharmaceuticals
  • Protein aggregation and stability
  • Therapeutic antibody development

Background:

  • Monoclonal antibodies (mAbs) are a rapidly expanding class of biological therapeutics.
  • Antibody aggregation is a significant challenge impacting the developability and efficacy of these protein-based drugs.
  • Aggregation arises from partial unfolding, leading to intermolecular associations and precipitate formation.

Purpose of the Study:

  • To review the relationship between the intrinsic sequence and structural properties of immunoglobulin G (IgG) and their susceptibility to unfolding and aggregation.
  • To discuss the influence of antibody domain structures on thermal stability and aggregation tendencies.
  • To explore strategies for mitigating antibody aggregation and review aggregation in antibody-drug conjugates (ADCs).

Main Methods:

  • Literature review focusing on the correlation between antibody sequence, structure, and aggregation.
  • Analysis of factors influencing antibody unfolding and domain stability.
  • Examination of aggregation mechanisms and mitigation strategies for mAbs and ADCs.

Main Results:

  • Antibody aggregation propensity is intrinsically linked to specific amino acid sequences and three-dimensional structures.
  • Antibody domain structures significantly affect thermostability and aggregation behavior.
  • Effective strategies exist to reduce aggregation, and ADC aggregation is influenced by multiple factors including DAR.

Conclusions:

  • Understanding the sequence-structure-aggregation relationship is crucial for developing stable monoclonal antibodies.
  • Targeting antibody domains and employing specific strategies can enhance therapeutic developability.
  • Further research into ADC aggregation mechanisms is needed for optimized conjugate design.