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Bacterial Inner-membrane Display for Screening a Library of Antibody Fragments
Published on: October 15, 2016
Structure-Guided Design of Antibodies
Justin A Caravella1, Deping Wang, Scott M Glaser
1Biogen Idec Inc., 12 Cambridge Center, Cambridge, MA 02142, USA. alexey.lugovskoy@biogenidec.com.
Current Computer-Aided Drug Design
|April 21, 2010
Summary
Structure-guided computational methods are advancing the design of monoclonal antibodies. These techniques optimize antibody affinity, specificity, and stability for improved biological applications.
Area of Science:
- Biochemistry
- Molecular Biology
- Immunology
Background:
- Monoclonal antibodies are established biological agents with high affinity and specificity for antigens.
- Hybridoma technology (1975) and advances in recombinant DNA, computational, and biophysical methods have deepened understanding of antibody sequence, structure, and function.
Purpose of the Study:
- To review recent successes in structure-guided computational methods for antibody design.
- To highlight the optimization of antibody affinity, specificity, and protein stability.
Main Methods:
- Structure-guided computational design approaches.
- Analysis of antibody sequence, structure, and function relationships.
- Application of recombinant DNA technologies.
Main Results:
- Demonstrated successes in designing antibodies and antibody-like molecules with enhanced properties.
- Optimized affinity and specificity to target antigens.
- Improved protein stability of designed antibody constructs.
Conclusions:
- Computational and biophysical methods are powerful tools for engineering antibodies.
- Structure-guided design enables the creation of antibodies with tailored biological and biophysical properties.
Related Concept Videos
01:10Antibody Structure
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...
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...
01:10Antibody Structure
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...
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...
01:25Antibody Structure and Classes
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.
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.