Ablynx.com / Nanobody® Bibliography

Three-dimensional structure of a Nanobody^®(modeled on the VHH with pdb-code 1U0Q, Cambillau et al). The target molecule is recognized by the surface formed by three hypervariable regions located at the top of the molecule (in green, cyan and blue). Hallmarks, amino acid residues that further differentiate a camelid VHH from a human VH, can be located at different positions within the framework regions, and here are coloured red, pink and magenta.

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Nanobody^® Bibliography > Tailored in vivo half-life

Nanobody^® Bibliography

Tailored in vivo half-life

Muyldermans S. Single domain camel antibodies: current status. J Biotechnol. 2001 Jun; 74 (4): 277-302.

Gibbs WW. Nanobodies. Sci Am. 2005 Aug; 293 (2): 78-83.
Harmsen MM, Van Solt CB, Fijten HP, Van Setten MC. Prolonged in vivo residence times of llama single-domain antibody fragments in pigs by binding to porcine immunoglobulins. Vaccine. 2005 Sep 30; 23 (41): 4926-34.

Coppieters K, Dreier T, Silence K, Haard HD, Lauwereys M, Casteels P, Beirnaert E, Jonckheere H, Wiele CV, Staelens L, Hostens J, Revets H, Remaut E, Elewaut D, Rottiers P. Formatted anti-tumor necrosis factor alpha VHH proteins derived from camelids show superior potency and targeting to inflamed joints in a murine model of collagen-induced arthritis. Arthritis Rheum. 2006 Jun; 54 (6): 1856-66.