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Related Concept Videos

Antibody Actions01:26

Antibody Actions

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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
Antibodies can bind to pathogens, preventing them from infecting host cells. This process...
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Affinity and Avidity01:41

Affinity and Avidity

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Antibody Structure and Classes01:25

Antibody Structure and Classes

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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.
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.
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Antibody Structure01:10

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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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Cross-reactivity00:42

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A Method of Targeted Cell Isolation via Glass Surface Functionalization
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Communication: Antibody stability and behavior on surfaces.

Derek B Bush1, Thomas A Knotts1

  • 1Department of Chemical Engineering, Brigham Young University, Provo, Utah 84602, USA.

The Journal of Chemical Physics
|August 17, 2015
PubMed
Summary

Antibody microarrays show poor reliability due to antibody-surface interactions. Collapsing onto hydrophobic surfaces reduces antibody stability and antigen recognition, impacting biosensor performance.

Area of Science:

  • Biophysics
  • Surface Science
  • Biotechnology

Background:

  • Antibody microarrays offer revolutionary potential for molecular detection in biosensors.
  • Current antibody microarray applications are hindered by poor reliability and performance.
  • Strong antibody-surface interactions are hypothesized to destabilize antibody structure and impede antigen recognition.

Purpose of the Study:

  • To investigate the impact of antibody-surface interactions on antibody structure and stability.
  • To understand how antibody orientation and surface properties affect performance in microarrays.

Main Methods:

  • Utilized a coarse-grain protein-surface model parameterized with experimental data.
  • Simulated antibody-surface interactions for two antibody orientations on hydrophobic and hydrophilic surfaces.

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Main Results:

  • Antibodies were observed to collapse onto hydrophobic surfaces, irrespective of attachment geometry.
  • Antibodies on hydrophobic surfaces exhibited significantly lower stability compared to those on hydrophilic surfaces or in solution.
  • These interactions create steric interference, hindering antigen recognition.

Conclusions:

  • Antibody collapse and reduced stability on hydrophobic surfaces are key factors contributing to poor microarray performance.
  • Understanding these dynamics offers insights for improving antibody microarray design and reliability.
  • This research provides a foundation for developing more stable and effective antibody-based biosensors.