Improving the pharmacokinetic properties of biologics by fusion to an anti-HSA shark VNAR domain.

ABSTRACT: Advances in recombinant antibody technology and protein engineering have provided the opportunity to reduce antibodies to their smallest binding domain components and have concomitantly driven the requirement for devising strategies to increase serum half-life to optimise drug exposure, thereby increasing therapeutic efficacy. In this study, we adopted an immunization route to raise picomolar affinity shark immunoglobulin new antigen receptors (IgNARs) to target human serum albumin (HSA). From our model shark species, Squalus acanthias, a phage display library encompassing the variable binding domain of IgNAR (VNAR) was constructed, screened against target, and positive clones were characterized for affinity and specificity. N-terminal and C-terminal molecular fusions of our lead hit in co

SUBMITTER: Muller MR 

PROVIDER: S-EPMC3502234 | biostudies-literature | 2012 Nov-Dec

REPOSITORIES: biostudies-literature