Difference between revisions of "Team:NTHU Formosa/Nanobody"

Nanobody

　 Nanobodies are single variable domain antibody fragments (VHH) derived from heavy-chain only antibodies discovered and identified in at least two types of organisms, camelidae (e.g., camel and llama) and cartilaginous fish (e.g., nurse shark and Wobbegong).

　 The molecular size of nanobody is about 3 nm (15kDa), 1/10000 of hair diameter. Such property earned it the name, nanobody. They are more hydrophilic than conventional antibodies. They withstand big pH variation. Their small size gives them the ability to penetrate the tissue faster and to reach deeper into the binding pockets of enzymes. Being able to refold after heat denaturation keeps nanobodies functional and active at 70°C or 2-hour 90°C heat shock.

　 Nanobodies retain full antigen binding capacity and are considerably stable. Conventional antibodies are composed with variable domains along with heavy chains and light chains. When binding with proteins, all three parts of them are necessarily involved. Hence, nanobodies’ comparably simple structure greatly increases their antigen binding affinity. What’s even better is that it’s less costly to make nanobodies than antibodies. According to the information from iCAN database (Institute collection and Analysis of Nanobody), over two thousand nanobodies are available for recognizing different antigens including molecular-bound molecules and soluble molecules.

　 Compared with antibodies, the unique features that nanobodies possess make them ideal for therapeutic and bioengineering tools. As a result, nanobodies are applied in our mechanism.