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.

Home R & D Nanobody® Bibliography > Tissue Penetration

Nanobody® Bibliography

Tissue Penetration

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.

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.