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Development and characterisation of synthetic ion channel binding proteins.

Project Description

We are developing methods to identify novel proteins, Affimers, that recognise extracellular domains of ion channels. These have applications in various aspects of biology, from tools to visualise the location and distribution of ion channels in native tissue, to novel modulators of ion channel function. As an example, we have developed Affimers that recognize the TRPV1 cation channel and enhance its activation by capsaicin (Tiede at al, 2017).

A PhD project is available to further develop this workwith the TRPV1-binding and other Affimers and establishing studies with native sensory neurons, tissue preparations, or clinical models of chronic pain. Tools can be developed for super-resolution imaging or purification of protein complexes. The pharmacological properties of TRPV1-binding Affimers can be further characterised in relation to other channel activation modalities, such as temperature and pH.

Funding Notes

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Tiede C, Bedford R, Heseltine SJ, Smith G, Wijetunga I, Ross R, et al. (2017) Affimer proteins are versatile and renewable affinity reagents. Elife 6, e24903.

Wrighton DC, Muench SP, Lippiat JD (2015) Mechanism of inhibition of mouse Slo3 (KCa 5.1) potassium channels by quinine, quinidine and barium. Br J Pharmacol 172, 4355-63.

Jin X, Shah S, Liu Y, Zhang H, Lees M, Fu Z, Lippiat JD, Beech DJ, Sivaprasadarao A, Baldwin SA, Zhang H, & Gamper N (2013) Activation of the Cl- Channel ANO1 by Localized Calcium Signals in Nociceptive Sensory Neurons Requires Coupling with the IP3 Receptor. Sci Signal 6, ra73.

How good is research at University of Leeds in Biological Sciences?

FTE Category A staff submitted: 60.90

Research output data provided by the Research Excellence Framework (REF)

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