Serge Muyldermans

TL;DR: The crystal structures of an antibody fragment derived from a camel heavy chain antibody against carbonic anhydrase, free and in complex with antigen are reported, Surprisingly, this single-domain antibody interacts with nanomolar affinity with the antigen through its third hypervariable loop (19 amino acids long).

TL;DR: The small size and strict monomeric behavior, in combination with other biochemical properties such as high solubility and high specificity and affinity for the cognate antigen, make single-domain antibodies ideal to design novel man-made conjugates harnessed with innovative effector functions outside the reach of classical antibodies.

TL;DR: This approach realizes the PSA detection at clinical relevant concentrations by introducing a sandwich assay involving a biotinylated secondary antibody and streptavidin modified gold nanoparticles.

TL;DR: The presence of the heavy‐chain antibodies and the possibility of immunizing a dromedary allows for the production of antigen binders consisting of a single domain only, which has two additional advantages: the camel or llama derived single domain antibodies might be an ideal scaffold for anti‐idiotypic vaccinations; and the development of smaller peptides or peptide mimetic drugs derived from of the antigen binding loops might be facilitated due to their less complex antigen binding site.

TL;DR: In this article, the use of variable fragments of immunoglobulins for passive immunotherapy or serotherapy was proposed, which are composed of at least one heavy chain variable fragment or derived therefrom, for therapeutic or veterinary purposes.