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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.
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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Conserved Binding Sites01:49

Conserved Binding Sites

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Many proteins’ biological role depends on their interactions with their ligands, small molecules that bind to specific locations on the protein known as ligand-binding sites. Ligand-binding sites are often conserved among homologous proteins as these sites are critical for protein function.
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Antigen receptors are essential components of the immune system crucial in defending the body against foreign invaders. These receptors are present on the surface of B and T cells, enabling them to recognize antigens and mount an appropriate immune response.
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Conservation of Protein Domains Over Different Proteins02:26

Conservation of Protein Domains Over Different Proteins

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Protein domains are small structurally independent units that are part of a single amino acid chain.  Although these domains are often structurally independent, they may rely on synergistic effects to perform their functions as part of a larger protein. Protein domains may be conserved within the same organism, as well as across different organisms.
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DNA as a Genetic Template02:05

DNA as a Genetic Template

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Two structural features of the DNA molecule provide a basis for the mechanisms of heredity: the four nucleotide bases and its double-stranded nature. The Watson-Crick model of double-helical DNA structure, proposed in 1952, drew heavily upon the X-ray crystallography work of researchers Rosalind Franklin and Maurice Wilkins. Watson, Crick, and Wilkins jointly received the Nobel Prize in Physiology or Medicine for their work in 1962. Franklin was, controversially, excluded from the prize for...
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Identification of Mouse and Human Antibody Repertoires by Next-Generation Sequencing
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DNA Framework Programmed Conformational Reconstruction of Antibody Complementary Determining Region.

Liqi Zhou1,2, Lei Ren2,3, Zhiang Bai2

  • 1National Laboratory of Solid State Microstructures, Jiangsu Key Laboratory of Artificial Functional Materials, College of Engineering and Applied Sciences and Collaborative Innovation Center of Advanced Microstructures, Nanjing University, Nanjing 210093, People's Republic of China.

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Researchers engineered artificial antibodies (DNFbodies) using DNA frameworks to precisely control complementary determining region (CDR) conformation. An optimized CDR loop span of ~2.3 nm significantly improved antibody-antigen binding affinity by threefold.

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Area of Science:

  • Biotechnology
  • Molecular Engineering
  • Immunology

Background:

  • Complementary determining regions (CDRs) are critical for antibody specificity and antigen binding.
  • Precise control over CDR conformation is essential for artificial antibody engineering but remains a challenge.
  • Existing methods lack programmable scaffolds for nanometer-level regulation of CDR conformation.

Purpose of the Study:

  • To develop a novel strategy for programming CDR conformation using DNA framework structures.
  • To create DNA framework-based artificial antibodies (DNFbodies) with tunable CDR loop spans.
  • To investigate the impact of CDR loop span on antibody-antigen binding affinity.

Main Methods:

  • Anchoring both ends of a free CDR loop to specific sites on a DNA framework.
  • Defining CDR loop spans with approximately 2 nm resolution.
  • Generating DNFbodies with systematically varied CDR loop spans.

Main Results:

  • Demonstrated precise control over CDR loop conformation via DNA framework anchoring.
  • Created DNFbodies exhibiting varied antibody-antigen binding affinities based on CDR loop span.
  • Identified an optimized CDR loop span (~2.3 nm) that enhanced binding affinity by approximately threefold compared to natural antibodies.

Conclusions:

  • The DNA framework strategy enables programmable regulation of CDR conformation with high precision.
  • Optimizing CDR loop span is critical for enhancing artificial antibody affinity.
  • This approach offers a promising route for the rational design of advanced artificial antibodies.