In the last decades, antibodies have become one of the most important and fastest growing classes of biotherapeutic proteins. Antibodies are Y-shaped proteins and consist of four polypeptide chains, i.e., two light and two heavy chains. The structure of an antibody can be subdivided into two antigen-binding fragments (Fabs) and a crystallizable fragment region (Fc). The crystallizable fragment region is responsible for interacting with the cell surface, activating the immune system and extending the half-life of an antibody, while the Fab can recognize a variety of different pathogens with high specificity.
The rational design of therapeutic antibodies strongly relies on the quality of antibody structures. However, the high flexibility of antibodies in solution influences their function and binding properties substantially. Therefore, in-depth understanding of antibody dynamics, i.e., the conformational diversity and the kinetics of conformational transitions, is essential for quantitative predictions of binding properties. Environmental influences, such as pH dependence, redox environment and temperature, can lead to structural and functional changes that in consequence affect antigen binding and recognition, e.g., in engineering anti-cancer antibodies the role of the pH plays a central role in determining the function and efficiency of antibodies. As antibody-based biologics evolve towards more elaborated forms, i.e., bi-specifics, specific engineered isotypes, multivalent and dedicated formats, a profound knowledge of intrinsic structural and biophysical properties is key for the next generation of therapeutics.
This Research Topic welcomes the submission of Original Research, Reviews or Perspective articles on all aspects related to the theme of conformational diversity of antibodies and implications for binding and function. This includes but is not limited to:
• Antibody structure prediction
• Antibody engineering
• Thermal Stability
• pH-dependent antibody functions
• Antibody affinity maturation
• Antibody-antigen recognition
• Antibody specificity and selectivity
• Antibody biophysical properties
Dr. Guy Georges is an employee and shareholder of Roche, which provides diagnostics and pharmaceuticals. All other Topic Editors declare no competing interests in relation to the topic.
In the last decades, antibodies have become one of the most important and fastest growing classes of biotherapeutic proteins. Antibodies are Y-shaped proteins and consist of four polypeptide chains, i.e., two light and two heavy chains. The structure of an antibody can be subdivided into two antigen-binding fragments (Fabs) and a crystallizable fragment region (Fc). The crystallizable fragment region is responsible for interacting with the cell surface, activating the immune system and extending the half-life of an antibody, while the Fab can recognize a variety of different pathogens with high specificity.
The rational design of therapeutic antibodies strongly relies on the quality of antibody structures. However, the high flexibility of antibodies in solution influences their function and binding properties substantially. Therefore, in-depth understanding of antibody dynamics, i.e., the conformational diversity and the kinetics of conformational transitions, is essential for quantitative predictions of binding properties. Environmental influences, such as pH dependence, redox environment and temperature, can lead to structural and functional changes that in consequence affect antigen binding and recognition, e.g., in engineering anti-cancer antibodies the role of the pH plays a central role in determining the function and efficiency of antibodies. As antibody-based biologics evolve towards more elaborated forms, i.e., bi-specifics, specific engineered isotypes, multivalent and dedicated formats, a profound knowledge of intrinsic structural and biophysical properties is key for the next generation of therapeutics.
This Research Topic welcomes the submission of Original Research, Reviews or Perspective articles on all aspects related to the theme of conformational diversity of antibodies and implications for binding and function. This includes but is not limited to:
• Antibody structure prediction
• Antibody engineering
• Thermal Stability
• pH-dependent antibody functions
• Antibody affinity maturation
• Antibody-antigen recognition
• Antibody specificity and selectivity
• Antibody biophysical properties
Dr. Guy Georges is an employee and shareholder of Roche, which provides diagnostics and pharmaceuticals. All other Topic Editors declare no competing interests in relation to the topic.
