Abstract
The reversible interaction between an affinity ligand and a complementary receptor has been widely explored in purification systems for several biomolecules. The development of tailored affinity ligands highly specific towards particular target biomolecules is one of the options in affinity purification systems. However, both genetic and chemical modifications on proteins and peptides widen the application of affinity ligand-tag receptor pairs towards universal capture and purification strategies. In particular, this chapter will focus on two case studies highly relevant for biotechnology and biomedical areas, namely, the affinity tags and receptors employed on the production of recombinant fusion proteins and the chemical modification of phosphate groups on proteins and peptides and the subsequent specific capture and enrichment, a mandatory step before further proteomic analysis.
Ana Sofia Pina and Íris L. Batalha have contributed equally to this work.
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Acknowledgments
The authors thank the financial support from Fundação para a Ciência e a Tecnologia through grant no. PEst-C/EQB/LA0006/2011 and contract nos. PTDC/EBB-BIO/102163/2008, PTDC/EBB-BIO/098961/2008, PTDC/EBB-BIO/118317/2010, SFRH/BD/48804/2008 for A.S.P., and SFRH/BD/64427/2009 for I.L.B., as well as to Santander Totta Bank—Universidade Nova de Lisboa for the Scientific Award 2009/2010.
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Pina, A.S., Batalha, Í.L., Roque, A.C.A. (2014). Affinity Tags in Protein Purification and Peptide Enrichment: An Overview. In: Labrou, N. (eds) Protein Downstream Processing. Methods in Molecular Biology, vol 1129. Humana Press, Totowa, NJ. https://doi.org/10.1007/978-1-62703-977-2_14
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