Antibody fragments Prolonging circulation half-life special issue-antibody research.docVIP

Advances in Bioscience and Biotechnology, 2013, 4, 689-698 ABB /10.4236/abb.2013.45090 Published Online May 2013 (/journal/abb/) Antibody fragments: Prolonging circulation half-life special issue-antibody research Annabelle Patricia Herrington-Symes , Monika Farys , Hanieh Khalili , Steve Brocchini 1 1 1,2 1,2 1 2 UCL School of Pharmacy, University College London, London, UK National Institute for Health Research (NIHR) Biomedical Research Centre at Moorfields Eye Hospital NHS, Foundation Trust and UCL Institute of Ophthalmology, London, UK Email: steve.brocchini@ucl.ac.uk Received 28 February 2013; revised 20 April 2013; accepted 15 May 2013 Copyright ? 2013 Annabelle Patricia Herrington-Symes et al. This is an open access article distributed under the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited. ABSTRACT Often the doses of the antibody used in therapy can be relatively high compared to other protein-therapeutics. When considering production as a limiting factor, solutions have included the production of antibody fragments such as Fab, Fv and scFv using microbial expression systems. These systems can provide greater amounts of the de- sired protein compared to earlier eukaryotic systems [1- 3]. Using prokaryotic expression systems can be very ef- ficient to produce antibody fragments due to their small size and lack of glycosylation [3]. Antibody fragments can display improved tissue pene- tration due to their smaller size compared to full anti- bodies. The lack of an Fc domain means antibody frag- ments have reduced half-lives and a lower immunoge- nicity risk. The Fc domain has two functions in a full IgG, these are: i) neonatal Fc receptor (FcRn) mediat