Custom Nanobody Development

Camelid single heavy chain antibodies and nanobodies:

In the late 1980s, students of Belgian scientist Dr. Hamers accidentally discovered that in addition to traditional IgG1 type antibodies, the serum of domesticated camels also contained about 75% of antibodies with only one heavy chain but no light chain. A new type of antibody has then been revealed: Heavy chain-only antibodies (HCAbs). This antibody is also expressed in a considerable proportion in alpacas (Llama and Alpaca). Subsequently, the N-terminal domain of the single heavy chain antibody was proven to directly bind to the antigen. This region similar to the VH domain of human IgG1 was named Single domain antibody (sdAb), VHH, or (Nanobody) Nanobody, and named after each This form is used in antibody drug development.

Advantages of camelid single heavy chain antibodies and nanobodies:

In order to compensate for the exposure of more heavy chain amino acid residues caused by the deletion of the light chain, camelid single heavy chain antibodies have improved their overall hydrophilicity during the evolution process, significantly improving their thermal stability and water solubility. Nanobodies can remain stable at as high as 70 ℃.
Although camels are relatively far apart from humans in terms of evolution, camel antibodies are much more homologous to human antibodies than rodents, which greatly reduces the risk of immunogenicity.
The CDR3 of camelid single heavy chain antibodies is longer than that of human and rodent antibodies. This feature makes camelid antibodies easier to penetrate and recognize deeply embedded epitopes.
The configuration of the single heavy chain greatly reduces the complexity of engineering modification, making affinity maturation, humanization modification, and bispecific antibody construction easier.
Nanobodies derived from alpaca single domain antibodies are only about 15Kd, and their extremely small size makes them easier to infiltrate into tissues.