Polymer-antibody fragment conjugates for biomedical applications

作者: Akshay Srivastava , Iain B. O’Connor , Abhay Pandit , J. Gerard Wall

DOI: 10.1016/J.PROGPOLYMSCI.2013.09.003

关键词:

摘要: Abstract Many proteins benefit from improved solubility, immunocompatibility, pharmacokinetics or stability upon conjugation to polymers. For protein-conjugates used in delivery imaging vivo , this can mean increased efficacies due longer circulatory half-lives intracellular stability. In vitro polymers increase stability, reduce aggregation, mediate multimerization phase separation of assay sensitivities improve signal detection. The emergence recombinant antibody technologies over the past two decades has allowed relatively simple isolation (human) fragments, such as Fabs and single chain variable fragments (scFvs), that retain binding properties their parent molecules may exhibit additional reduced immunogenicity, tissue penetration packing density on sensor surfaces small sizes. addition, protein engineering approaches facilitate chemical functionalization have seen linked a broad spectrum chemically functionally diverse polymeric molecules. Of varied strategies polymer–protein coupling, amine cysteine are most widely applied chemistries with fragments. Simple poly(ethyleneglycol) half-life, decrease renal clearance, aggregation without compromising antigen binding. Meanwhile, be control coupling responsive enable context release drug payload polymer–antibody fragment complex. Recent years conjugates increasingly encroach into areas traditionally associated monoclonal antibody–polymers we discuss potential conjugates, applications delivery, engineering, diagnostics bioseparation.

参考文章(213)
J. Milton Harris, M. R. Sedaghat-Herati, Preparation and use of polyethylene glycol propionaldehyde ,(1990)
Zheng-Rong Lu, Pavla Kopečková, Jindřich Kopeček, Polymerizable Fab' antibody fragments for targeting of anticancer drugs. Nature Biotechnology. ,vol. 17, pp. 1101- 1104 ,(1999) , 10.1038/15085
Masao Inagake, Toshio Takahashi, Kazuya Kitamura, Ken-ichiroh Takashina, Akinori Noguchi, Toshiharu Yamaguchi, Hiroshi Tsurumi, Sen-ichiroh Hakomori, Akira Noguchi, Tatsushi Toyokuni, Chemical Engineering of the Monoclonal Antibody A7 by Polyethylene Glycol for Targeting Cancer Chemotherapy Cancer Research. ,vol. 51, pp. 4310- 4315 ,(1991)
GlenJ McIntyre, GregoryC Fanning, Design and cloning strategies for constructing shRNA expression vectors BMC Biotechnology. ,vol. 6, pp. 1- 8 ,(2006) , 10.1186/1472-6750-6-1
Alexander Kabanov, Jian Zhu, Valery Alakhov, Pluronic Block Copolymers for Gene Delivery Advances in Genetics. ,vol. 53, pp. 231- 261 ,(2005) , 10.1016/S0065-2660(05)53009-8
Saulius Juodkazis, Naoki Mukai, Ryosuke Wakaki, Akira Yamaguchi, Shigeki Matsuo, Hiroaki Misawa, Reversible phase transitions in polymer gels induced by radiation forces Nature. ,vol. 408, pp. 178- 181 ,(2000) , 10.1038/35041522
Elizabeth Tully, Seamus P. Higson, Richard O’Kennedy, The development of a 'labeless' immunosensor for the detection of Listeria monocytogenes cell surface protein, Internalin B. Biosensors and Bioelectronics. ,vol. 23, pp. 906- 912 ,(2008) , 10.1016/J.BIOS.2007.09.011
Stefan Schreiber, Paul Rutgeerts, Richard N Fedorak, Munaa Khaliq–Kareemi, Michael A Kamm, Michel Boivin, Charles N Bernstein, Michael Staun, Ole Østergaard Thomsen, Alison Innes, CDP870 Crohn’s Disease Study Group, None, A randomized, placebo-controlled trial of certolizumab pegol (CDP870) for treatment of Crohn's disease Gastroenterology. ,vol. 129, pp. 807- 818 ,(2005) , 10.1053/J.GASTRO.2005.06.064