Generally, in order to determine protein structures, scientists make use of solid samples, particularly crystals, using X-ray or frozen solutions through electron microscopy. However, the problem is that crystals are at times difficult to acquire. Not only that, but proteins also work in a liquid state, which causes their shape and mobility to differ from the solid state, especially when it comes to small species.
To tackle this problem, researchers have been successful in using Nuclear Magnetic Resonance (NMR) techniques to identify the structure of a specific nanobody, Nb23. The breakthrough is considerably huge for Nuclear Magnetic Resonance (NMR) Market as it could lead to an enhanced understanding in which the small protein is derived from an antibody. These types of antibodies have only been found in camelids (i.e., llamas, alpacas, and camels) and sharks and have the ability to fight various kinds of diseases such as psoriasis, breast cancer, psoriasis, arthritis, and lymphoma.
Through the use of NMR spectroscopy, the researchers would be able to map out all the relevant factors of nanobody function. Further, they can recognize the changes that arise when the nanobody binds to its target proteins and prevents the formation of amyloid (abnormal protein aggregation) that results in the occurrence of functional or degenerative diseases.
The team is quite eager to investigate the potential of nano bodies in contrast to disease-fighting monoclonal antibodies. They are the proteins made in the laboratory to imitate the immune system’s power to fight off harmful antigens like viruses. However, they are extremely hard to handle and difficult to conserve and, at times, can also penetrate the solid tissue because of their size. In comparison, nanobodies are tenfold smaller in size and provide stability, good solubility, strong binding affinity, and biocompatibility. It is mainly due to their natural origin, thus indicating that they might have great potential as alternatives for therapeutic use.
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