Antibody-Antigen Complexes

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Antibodies, large proteins produced by the immune system, are composed of two identical heavy chains and two identical light chains. These chains are connected by disulfide bonds within and between them, resulting in a distinctive Y-shaped structure. The antigen binding site is positioned at the tips of the Y-shaped arms.

At this binding site, specific amino acid sequences called complementarity determining regions (CDRs) play a pivotal role in precisely recognizing and binding to the antigen. These CDRs showcase remarkable diversity and variability, enabling antibodies to target antigens with exceptional specificity.

When an antibody binds to its specific antigen, a complex interplay of various molecular forces, including electrostatic interactions, hydrogen bonding, van der Waals forces, and hydrophobic interactions come into play. Understanding this intricate molecular recognition process is paramount in the development of efficacious therapeutic antibodies and the creation of targeted treatments.

Epitope mapping is a crucial process in antibody characterization, and it plays a significant role in understanding the specificity, function, and potential applications of antibodies. Epitopes are the specific regions on antigens (such as proteins, peptides, or other molecules) that antibodies recognize and bind to. Mapping these epitopes provides valuable insights into how antibodies interact with their targets and helps researchers and scientists in various ways, such as understanding the antibody specificity, guiding rational design and securing and protecting patents related to antibodies, vaccines, and other biotechnological products.

Confidently solve antibody-antigen complexes with cryo-EM.

At NanoImaging Services, we recognize the vital role played by structural biology in understanding antibody-antigen complexes. These complexes hold the key to developing effective antibody therapeutics and vaccines, and understanding their precise interactions is essential for advancing medical research. Our experts use cryo-EM to provide high-resolution epitope mapping of antibody- and FAB-antigen complexes. Cryo-EM can provide structural details that enable us to better describe and characterize these complex biological systems.

Start with a feasibility assessment to gain crucial structural insights in under two weeks, or use our epitope mapping service to identify the precise region where antibodies bind to antigens, revealing atomic interactions and conformational changes that may influence the mechanism of action of therapeutic agents. 

In addition to cryo-EM, we also employ negative stain transmission electron microscopy (TEM) workflows for additional analysis. While negative stain TEM provides lower resolution compared to cryo-EM, it is still valuable in validating the integrity of antigen-antibody complexes and identifying specific regions of the antigen recognized by antibodies. 

This multi-faceted approach, combining 2D classifications from negative stain TEM with high-resolution 3D cryo-EM models and maps, allows researchers to gain a comprehensive understanding of the intricate structure of antibody-antigen and how they interact.

NIS is committed to providing the highest level of expertise and support to ensure the success of your project. Our clients trust us to help them unlock the structural details of their antibody-antigen complexes and gain a deeper understanding of their mechanisms of action. 

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