Skip to content

Research at St Andrews

Isolation of isoform-specific binding proteins (Affimers) by phage display using negative selection

Research output: Contribution to journalArticle

Author(s)

Anna Ah-San Tang, Christian Tiede, David J Hughes, Michael J McPherson, Darren C Tomlinson

School/Research organisations

Abstract

Some 30 years after its discovery, phage display remains one of the most widely used methods of in vitro selection. Initially developed to revolutionize the generation of therapeutic antibodies, phage display is now the first choice for screening artificial binding proteins. Artificial binding proteins can be used as reagents to study protein-protein interactions, target posttranslational modifications, and distinguish between homologous proteins. They can also be used as research and affinity reagents, for diagnostic purposes, and as therapeutics. However, the ability to identify isoform-specific reagents remains highly challenging. We describe an adapted phage display protocol using an artificial binding protein (Affimer) for the selection of isoform-selective binding proteins.

Close

Details

Original languageEnglish
Article numbereaan0868
Number of pages12
JournalScience Signaling
Volume10
Issue number505
DOIs
Publication statusPublished - 14 Nov 2017

Discover related content
Find related publications, people, projects and more using interactive charts.

View graph of relations

Related by author

  1. Analysis of paramyxovirus transcription and replication by high-throughput sequencing

    Wignall-Fleming, E. B., Hughes, D. J., Vattipally, S., Modha, S., Goodbourn, S., Davison, A. J. & Randall, R. E., 12 Jun 2019, In : Journal of Virology.

    Research output: Contribution to journalArticle

  2. Contribution of the KSHV and EBV lytic cycles to tumourigenesis

    Manners, O., Murphy, J., Coleman, A., Hughes, D. J. & Whitehouse, A., Oct 2018, In : Current Opinion in Virology. 32, p. 60-70

    Research output: Contribution to journalReview article

  3. Generation of specific inhibitors of SUMO1- and SUMO2/3-mediated protein-protein interactions using Affimer (Adhiron) technology

    Hughes, D. J., Tiede, C., Penswick, N., A. S. Tang, A., Trinh, C. H., Mendal, U., Zajac, K. Z., Gaule, T., Howell, G., Edwards, T. A., Duan, J., Feyfant, E., McPhereson, M. J., Tomlinson, D. C. & Whitehouse, A., 14 Nov 2017, In : Science Signaling. 10, 505, 14 p., eaaj2005.

    Research output: Contribution to journalArticle

  4. ARID3B: a novel regulator of the Kaposi’s sarcoma-associated herpesvirus lytic cycle

    Wood, J., Boyne, J., Paulus, C., Jackson, B., Nevels, M. M., Whitehouse, A. & Hughes, D. J., Oct 2016, In : Journal of Virology. 90, 20, p. 9543-9555

    Research output: Contribution to journalArticle

  5. Gammaherpesvirus infection modulates the temporal and spatial expression of SCGB1A1 (CCSP) and BPIFA1 (SPLUNC1) in the respiratory tract

    Leeming, G. H., Kipar, A., Hughes, D. J., Bingle, L., Bennett, E., Moyo, N. A., Tripp, R. A., Bigley, A. L., Bingle, C. D., Sample, J. T. & Stewart, J. P., Jun 2015, In : Laboratory Investigation. 95, p. 610-624 15 p.

    Research output: Contribution to journalArticle

Related by journal

  1. Generation of specific inhibitors of SUMO1- and SUMO2/3-mediated protein-protein interactions using Affimer (Adhiron) technology

    Hughes, D. J., Tiede, C., Penswick, N., A. S. Tang, A., Trinh, C. H., Mendal, U., Zajac, K. Z., Gaule, T., Howell, G., Edwards, T. A., Duan, J., Feyfant, E., McPhereson, M. J., Tomlinson, D. C. & Whitehouse, A., 14 Nov 2017, In : Science Signaling. 10, 505, 14 p., eaaj2005.

    Research output: Contribution to journalArticle

  2. Reconstituted human TPC1 is a proton-permeable ion channel and is activated by NAADP or Ca2+

    Pitt, S. J., Lam, A. K. M., Rietdorf, K., Galione, A. & Sitsapesan, R., 20 May 2014, In : Science Signaling. 7, 326, ra46.

    Research output: Contribution to journalArticle

ID: 251600611