Therapeutics
which can extend development timelines and increase costs.
Antibody alternatives
Engineered affinity reagents are growing in popu- larity for use in research and development applica- tions, designed to overcome the apparent limita- tions of antibodies. Comprising both nucleic acid and protein molecules, which adopt a defined con- formation that matches a binding surface on the target, it is possible to achieve high affinity specific interactions with great specificity18. While many examples of affinity reagents have entered the mar- ketplace for research and therapeutic purposes (Table 1), a scaffold particularly well-suited for commercial anti-ID applications is the Affimer® protein.
Affimer binders are screened and selected from phage libraries, allowing targeting towards certain antigens and the isolation of high affinity binders that specifically identify either free or bound ther- apeutic antibodies. As this recombinant scaffold contains no post-translational modifications or disulphide bonds, production within inexpensive prokaryotic systems is simple, and batch-to-batch reproducibility is assured, reducing regulatory issues with the incorporation of this reagent into PK assays, for use throughout a project lifecycle23. A significant benefit of Affimer proteins over other available anti-ID reagents appears to be the lack of requirement for affinity maturation of selected binders. A number of molecules have been developed that show excellent specificity to indi- vidual therapeutic antibodies, with complete selec- tion and characterisation of the binders possible within just three months. These benefits would clearly offer reduced development and production costs, while maintaining the high-quality charac- teristics of the resulting reagent to ensure accurate and reliable bioanalytical assay results. DDW
Dr Robert Ford works as a Senior Scientist in the Validation team at Avacta Life Sciences. His exper- tise is used to generate data using Affimer technol- ogy in customer, internal and collaborative pro- jects. Rob is from a Biochemistry and Molecular Biology background, his PhD involved investigat- ing (+)ssRNA icosahedral virus assembly and dis- assembly mechanisms in model viral systems.
Dr Toni Hoffman obtained his PhD at the Max- Planck Institute of Molecular Plant Physiology. His interest in protein engineering and design led him to Leeds University where he developed
Drug Discovery World Winter 2017/18 13
Affimer precursors, and he then joined Avacta as a Senior Scientist. As part of the R&D team, Toni is involved in projects focusing on the use of Affimers in diagnostic assays.
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