Ms Anna Tang

BSc Hons Molecular Biology (Newcastle University, 2002)
Research Technician
School of Molecular and Cellular Biology

Contact: Astbury 7.103 / 7.106 / 7.110, +44(0) 113 34 33025, email address for  

I am the senior research technician for the BioScreening Technology Group (BSTG). The BSTG developed a non-antibody scaffold protein called Adhiron (now known as Affimer), which constrains one or two variable peptide sequences for molecular recognition purposes. Phage display libraries of Affimers can be screened against a wide range of target molecules to identify specific binders. The BSTG has formed collaborative partnerships with academics, clinicians and industry to develop Affimers as reagents for R&D, diagnostics, and therapeutics. We work closely with Avacta Life Sciences where Affimer technology is commercialised.

As well as working full-time, I am also a part-time PhD student (from October 2015). My project is to target SH3 domains with Affimers and use them to study protein-protein interactions in cell signalling pathways implicated in human cancers.

Previous to my career at the University of Leeds, I have been employed as a research and development scientist in both industry, and academia, and now have 15 years’ experience in the fields of bioscience.

Connect with me on LinkedIn: www.linkedin.com/in/anna-tang-69682376

Publications:

Tang AAS, Tiede C, Hughes DJ, McPherson MJ and Tomlinson DC. Isolation of isoformspecific binding proteins (Adhirons/Affimers) by phage display using negative selection. Sci. Signal. 10, eaan0868 (2017). https://doi.org/10.1126/scisignal.aan0868

Hughes DJ, Tiede C, Penswick N, Tang AAS, Trinh CH, Mandal U, Zajac KZ, Gaule T, Howell G, Edwards TA, Duan J, Feyfant E, M. McPherson MJ, Tomlinson DC and Whitehouse A. Generation of specific inhibitors of SUMO1- and SUMO2/3-mediated protein-protein interactions using Affimer (Adhiron) technology. Sci. Signal. 10, eaaj2005 (2017). https://doi.org/10.1126/scisignal.aaj2005

Tiede C, Tang AA, Deacon SE, Mandal U, Nettleship JE, Owen RL, George SE, Harrison DJ, Owens RJ, Tomlinson DC and McPherson MJ. Adhiron: a stable and versatile peptide display scaffold for molecular recognition applications. Protein Eng Des Sel, 2014, 27(5):145-55. https://doi.org/10.1093/protein/gzu007

Rawlings AE, Bramble JP, Tang AAS, Somner LA, Monnington AE, Cooke DJ, McPherson MJ, Tomlinson DC and Staniland SS. Phage display selected magnetite interacting Adhirons for shape controlled nanoparticle synthesis. Chemical Science, 2015, 6, 5586-5594. https://doi.org/10.1039/C5SC01472G

Koutsoumpeli E, Tiede C, Murray J, Tang A, Bon RS, Tomlinson DC and Johnson S. Antibody Mimetics for the Detection of Small Organic Compounds Using a Quartz Crystal Microbalance. Analytical Chemistry, 201789, 3051−3058. https://doi.org/10.1021/acs.analchem.6b04790

Sharma R, Deacon SE, Nowak D, George SE, Szymonik MP, Tang AA, Tomlinson DC, Davies AG, McPherson MJ and Wälti C. Label-free electrochemical impedance biosensor to detect human interleukin-8 in serum with sub-pg/ml sensitivity. Biosensors and Bioelectronics, 2016, 80, 607-613. https://doi.org/10.1016/j.bios.2016.02.028

Tiede C, Bedford R, Heseltine SJ, Smith G, Wijetunga I, Ross R, AlQallaf D, Roberts AP, Balls A, Curd A, Hughes RE, Martin H, Needham SR, Zanetti-Domingues LC, Sadigh Y, Peacock TP, Tang AA, Gibson N, Kyle H, Platt GW, Ingram N, Taylor T, Coletta LP, Manfield I, Knowles M, Bell S, Esteves F, Maqbool A, Prasad RK, Drinkhill M, Bon RS, Patel V, Goodchild SA, Martin-Fernandez M, Owens RJ, Nettleship JE, Webb ME, Harrison M, Lippiat JD, Ponnambalam S, Peckham M, Smith A, Ferrigno PK, Johnson M, McPherson MJ, Tomlinson DC. Affimer proteins are versatile and renewable affinity reagents. eLife, 2017, 6:e24903. https://doi.org/10.7554/eLife.24903.001

Martin HL, Bedford R, Heseltine SJ, Tang AA, Haza KZ, Rao A, McPherson MJ, Tomlinson DC. Non-immunoglobulin scaffold proteins: Precision tools for studying protein-protein interactions in cancer. New Biotechnology, 2018, S1871-6784 (17) 30541-1. https://doi.org/10.1016/j.nbt.2018.02.008