Nanobody

A nanobody is a functional antigen-binding fragment derived from a single heavy chain of an immunoglobulin, typically from camelids such as llamas and alpacas. Unlike conventional antibodies which are composed of both heavy and light chains, nanobodies consist solely of a single variable domain (VHH) and a constant domain (CH2 and CH3). This simplified structure confers several advantageous properties.

These unique attributes include a small molecular size, which allows for enhanced tissue penetration and access to challenging targets. Nanobodies also exhibit high stability under various conditions, including extreme temperatures and pH. Their single-domain nature means they can be easily engineered and produced using recombinant DNA technology in various expression systems, such as bacteria or yeast, leading to cost-effective and scalable production.

The therapeutic potential of nanobodies is extensive. They can be employed as diagnostic tools, imaging agents, and therapeutics. In therapy, they can neutralize toxins, block protein-protein interactions, deliver payloads like drugs or radioisotopes, and act as agonists or antagonists for specific cellular receptors. Their versatility has led to their development for a wide range of diseases, including cancer, infectious diseases, and inflammatory disorders. Research continues to explore novel applications and optimize nanobody design for improved efficacy and specificity.