Based on their simple structure, their good binding properties and their possibility of effective expression in Echeriachia coli camelid VHH domains from synthetic anti-body libraries find increasing applications in diagnostics and therapies.
Selection and characterisation of VHH domains against surface proteins of immune cells
Using the phage display technique, we select a camelid VHH domain that is targeted against a tumour-relevant receptor protein of an immune cell.
Application of the VHH domain B10 for the imaging of systemic Amyloidosis
We further used the phage display technology to generate the antibody fragment B10. This VHH is directed against amyloid fibrils, which are associated with pathology of many neurodegenerative and systemic diseases (for example Alzheimer’s disease and AA amyloidosis). Recombinant availability of B10 VHH antibody facilitates genetic fusion to alkaline phosphatase. This leads to enhanced binding affinity and allows easy detection with immunoassays. B10 antibody will be analyzed further to be applied in PET/CT imaging studies.