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Optimization and development of functionally active anti-Cdc42/Ras peptides

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  • Full or part time
    Dr Darerca Owen
  • Application Deadline
    No more applications being accepted

Project Description

A fully funded 4-year BBSRC-DTP Industrial CASE PhD studentship is available, commencing in October 2017, to develop peptide-based therapeutics designed to target Ras-driven cancers. The project builds on a considerable body of data generated in the academic research group led by Drs Darerca Owen and Helen Mott investigating the structure, thermodynamics and functions of small G protein-effector complexes, which has led to the development of candidate peptide therapeutics. The aim of the BBSRC-DTP Industry CASE awards is to provide PhD students with a first class, challenging training experience within the context of a mutually beneficial collaboration between academic and non-academic partner organizations. This project is partnered by MedImmune, a world-leading company specializing in antibody and peptide therapeutics, based just outside Cambridge. The work will use MedImmune’s considerable experience to optimize peptides for use as cellular probes and as anti-cancer lead therapeutic molecules. Candidate peptides will be tested in the Owen/Mott laboratory using a range of biophysical and biochemical assays. Those peptides with desired properties will be taken into cell-based assays to test their effects on Ras signalling and transformation. The project will provide a thorough training in a wide range of state-of-the-art techniques: advanced peptide chemistry and high-throughput screening techniques; molecular biology, protein biochemistry, biophysics and NMR for protein-protein interaction analysis; cell culture assays e.g. cell proliferation, anchorage-independent growth and focus formation assays.

The successful candidate will join the group led by Drs Darerca Owen and Helen Mott ( in the Department of Biochemistry, University of Cambridge and will be part of the Antibody Discovery and Protein Engineering (ADPE) department at MedImmune, working alongside a skilled team of scientists in a dynamic biotech environment, supervised by Dr Jeff Revell (

Funding Notes

Applicants should hold or be about to achieve a First/Upper-Second (2.i) class degree in a relevant subject. BBSRC studentships are available to UK nationals/EU students who meet UK residency requirements (see

The successful candidate will receive a stipend at RCUK rates for 4 years (£14,296 per annum for 2016-17) and in addition will benefit from a £2,500 per annum stipend enhancement; fees will be met in full.

Applications to Dr Darerca Owen ([email protected]) by 16th December 2016, enclosing a cover letter, a detailed curriculum vitae and the names and contact details of two academic referees.


Rittinger, K. et al.(1997) Crystal Structure of a small G protein in complex with the GTPase-activating protein RhoGAP. Nature 388:693

Mott, H.R., et al.(1999) Structure of the small G protein Cdc42 bound to the GTPase-binding domain of ACK Tyrosine Kinase. Nature 399:384.

Morreale, A. et al.(2000) Structure of Cdc42 complexed with the GTPase binding domain of PAK. Nat.Struct.Biol. 7:384

Mott, H.R. et al.(2003) Structure of the GTPase-Binding domain of Sec5 and Investigation of its Ral-binding Site J.Biol.Chem 278:17053

Owen, D. et al.(2003) Molecular dissection of the interaction between the small G proteins Rac1 and RhoA and Protein Kinase C Related Kinase 1 (PRK1) J.Biol.Chem. 278:50578

Elliot-Smith, A.E. et al.(2005) Specificity Determinants on Cdc42 for binding its effector protein ACK Biochemistry 44:12373

Elliot-Smith, A.E. et al.(2007) Double mutant cycle thermodynamic analysis of the hydrophobic Cdc42-ACK protein:protein interaction Biochemistry 46:14087

Modha, R. et al.(2008) The Rac1 Polybasic Region Is Required for Interaction with Its Effector PRK1 J.Biol.Chem. 283:1492

Owen, D. et al.(2008) The IQGAP1-Rac1 and IQGAP1-Cdc42 Interactions: Interfaces differ between the complexes J.Biol.Chem. 283:1692

Mott, H.R. and Owen, D.(2009) 'Structure of Rho Family Targets' Handbook of Cell Signalling 2:1827

Fenwick, R.B. et al.(2010) The RalB-RLIP76/RalBP1 complex reveals a novel mode of Ral-effector interaction. Structure 18:985

Hutchinson, C.L. et al.(2011) Mutational analysis reveals a single binding interface between RhoA and its effector, PRK1. Biochemistry 50:2860

Rajasekar, K.V. et al.(2013) The structure of the RLIP76 (RalBP1) RhoGAP domain-Ral binding domain dyad: fixed position of the domains leads to dual engagement of small G proteins at the membrane. Structure 21:2131

Hutchinson, C.L. et al.(2013) Differential binding of RhoA, B and C to the PRK isoforms PRK1, 2 and 3: PRKs have highest affinity for RhoB. Biochemistry 52:7999

Mott, H.R.&Owen, D.(2014) Structure and Function of RLIP76 (RalBP1): an intersection point between Ras and Rho signalling. Biochemical Society Transactions 42:52

Campbell, L. et al.(2015) Thermodynamic mapping of effector protein interfaces with RalA and RalB. Biochemistry 54:1380

Mott, H.R.&Owen, D.(2015) Ras superfamily Effector Complexes: What have we learned in two decades? Critical Reviews in Biochemistry and Molecular Biology 50:85

Watson, J.R. et al.(2016) Investigation of the Interaction Between Cdc42 and its Effector TOCA1: Handover of Cdc42 to the Actin Regulator N-WASP is Facilitated by Differential Binding Affinities. J. Biol. Chem. 291:13875

Thomas, J.T. et al.(2016) Inhibition of Ral GTPases using a stapled peptide approach. J. Biol. Chem. 291:18310

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

FTE Category A staff submitted: 189.63

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