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.

Home

R & D

Nanobody^® Bibliography > High Solubility and no Tendency to Aggregate

Nanobody^® Bibliography

High Solubility and no Tendency to Aggregate

Hamers-Casterman C, Atarhouch T, Muyldermans S, Robinson G, Hamers C, Bajyana Songa E, Bendahman N, Hamers R. Naturally occurring antibodies devoid of light chains. Nature 1993 June 3; 363 (6428): 446-8.

Davies J, Riechmann L. Single antibody domains as small recognition units: design and in vitro antigen selection of camelised, human VH domains with improved protein stability. Protein Eng. 1996 Jun; 9(6): 531-7.

Muyldermans S, Cambillau C, Wyns L. Recognition of antigens by single-domain antibody fragments: the superfluous luxury of paired domains. Trends Biochem Sci. 2001 Apr;26(4):230-5.

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

Nguyen VK, Desmyter A, Muyldermans S. Functional heavy-chain antibodies in Camelidae. Adv Immunol. 2001; 79: 261-96.

Conrath K, Vincke C, Stijlemans B, Schymkowitz J, Decanniere K, Wyns L, Muyldermans S, Loris R. Antigen binding and solubility effects upon the veneering of a camel VHH in framework-2 to mimic a VH. J Mol Biol. 2005 Jul 1; 350 (1): 112-25.

Gibbs WW. Nanobodies. Sci Am. 2005 Aug; 293 (2): 78-83.