Opportunities

The Tate group is seeking two talented new technicians. The positions will be funded by the GSK supported Fleming Initiative to combat antimicrobial resistance (AMR). These roles will support the generation of high-throughput mass spectrometry (MS) data to power state-of-the-art Artificial Intelligence (AI) and Machine Learning (ML) models to build a chemical ‘rule book’ for small molecule accumulation in bacteria.

Fleming Initiative Technician in High-Throughput Screening

Your role will focus on optimising and delivering high-throughput cellular screening assays to quantify small molecule accumulation within bacteria. The data generated from these experiments will feed into the development of state-of-the-art Artificial Intelligence (AI) and Machine Learning (ML) models to build a chemical ‘rule book’ for small molecule accumulation in bacteria. You will be contributing to a dynamic and ambitious Grand Challenge Project, funded by GSK and the Fleming Initiative, and you will work closely with multidisciplinary teams, from assay design and microbiology (Dr Andrew Edwards) to data science (Dr Marko Storch) and AI/ML (Prof. Alessandra Russo, Prof. Ramon Villar, Prof. Mauricio Barahona). In addition to your research activities, you will support the day-to-day running of the laboratory. This includes maintaining equipment, purchasing and organising consumables, disposal of biohazard and chemical waste, participating in laboratory duty rotas, and providing introductory training for new facility users.

Starting in February 2026 (or as soon as possible thereafter). Full time, fixed term, for up to 30 months in the first instance.

To apply, or for more information visit this link

Fleming Initiative Technician in High-Throughput Mass Spectrometry

Your role will focus on optimising and delivering high-throughput rapid mass spectrometry methods to quantify small molecules within complex bacterial cell lysates. The data generated from these experiments will feed into the development of state-of-the-art Artificial Intelligence (AI) and Machine Learning (ML) models to build a chemical ‘rule book’ for small molecule accumulation in bacteria. You will be contributing to a dynamic and ambitious Grand Challenge Project, funded by GSK and the Fleming Initiative, and you will work closely with multidisciplinary teams, from assay design and microbiology (Dr Andrew Edwards) to data science (Dr Marko Storch) and AI/ML (Prof. Alessandra Russo, Prof. Ramon Villar, Prof. Mauricio Barahona). In addition to your research activities, you will support the day-to-day running of the laboratory. This includes maintaining equipment, purchasing and organising consumables, disposal of biohazard and chemical waste, participating in laboratory duty rotas, and providing introductory training for new facility users.

Starting in February 2026 (or as soon as possible thereafter). Full time, fixed term, for up to 30 months in the first instance.

To apply, or for more information visit this link

[1+3] MRes + PhD Studentship for October 2026 - Understanding Antibody Uptake to Improve Antibody–Drug Conjugates (ADCs)

Antibody–drug conjugates (ADCs) are often described as “magic bullets” because they deliver toxic payloads selectively to cells that display a chosen antigen. In reality, they can also enter cells that lack the antigen, through routes that are not yet fully understood. This off-target uptake reduces safety and effectiveness, and it is a major challenge for the field.

In this PhD you will investigate the chemical and structural features that control ADC uptake and intracellular behaviour. You will design antibody and ADC variants by altering features such as isotype, surface charge, glycosylation, antigen binding affinity, and the type of payload and linker. You will then test how these changes affect uptake and routing to endosomes, recycling pathways, or the cytosol.

Supervisors: Dr Francesco Aprile, Department of Chemistry, Imperial, Professor Ed Tate, Department of Chemistry, Imperial, Dr Joanne McGregor, Director, Head of ADC Platform team at GSK

To apply, or for more information visit this link

[1+3] MRes + PhD Studentship for October 2026 - Cysteine-selective bioconjugation warheads for ADCs

Antibody-drug-conjugates (ADCs) are promising therapeutic modalities enabling the selective delivery of highly potent payloads to a disease tissue. ADCs are often coined “magic bullets” referring to their intrinsic targeting nature that results in deeper, on-target exposure of the payload and increased therapeutic window and have resulted in 17 approved ADC medicines to date. An ADC comprises of four key components: the antibody that drives tissue selectivity, a chemical warhead to attach onto the antibody’s native amino acids, a linker and a pharmaceutically active payload. Out of these marketed ADCs, 11 utilize cysteine capping conjugation employing a maleimide as the electrophilic chemical warhead. While highly selective for cysteines and offering fast rates of conjugation, the maleimide linkages can suffer from issues of buffer or serum instability resulting in deconjugation of the linker-payload and diminishing drug-antibody-ratio (DAR) over time.

This project will develop alternative cysteine selective, non-reversible capping bioconjugation warheads to overcome the intrinsic reversibility problems of maleimides on antibodies. Moreover, highly functionalisable warheads will be developed to enable the incorporation of one or multiple linkers and payloads leading to higher DAR or dual-payload ADCs. This project will assess the feasibility and utility of novel warhead structures to use as ADC conjugation chemistry, aiming to provide improved options for antibody conjugation. 

Supervisors: Professor James Bull, Department of Chemistry, Imperial, Professor Ed Tate, Department of Chemistry, Imperial, Dr  David Battersby, GSK, Dr Karina Chan, GSK.

To apply, or for more information visit this link

[1+3] MRes + PhD Studentship for October 2026 - Proteome-wide molecular glue discovery unlocked by chemical proteomics and machine learning

Molecular glues are transforming the landscape of drug discovery. By inducing or stabilising protein–protein interactions, they can modulate targets long considered “undruggable”, offering powerful new ways to reprogramme cellular networks. Unlike traditional inhibitors or PROTACs, molecular glues are small, drug-like molecules with the potential for exquisite selectivity and pharmacological breadth. Yet their discovery remains largely serendipitous, limited by the absence of high-throughput screening platforms and structural data essential for rational design.

This project will pioneer a breakthrough molecular glue discovery platform: an integrated proteomic and computational workflow capable of mapping the interactions of all proteins against all proteins in the cell, in the presence of thousands of potential glues. By coupling chemical proteomics to advanced computational deconvolution, we will generate the first large-scale database of molecular glue induced protein–protein interactions. High-throughput modelling and machine learning will then transform low-resolution proteomic signatures into high-resolution models of ternary complexes at scale, revealing the molecular logic of induced proximity and unlocking a new era of rational glue design.

Supervisors: Professor Ed Tate, Department of Chemistry, Imperial, Professor Christian Speck, Institute of Clinical Sciences, Imperial Faculty of Medicine, Dr Jack Houghton, Department of Chemistry, Imperial, Dr Rosa Cookson, Associate Director, Chemical Biology at Ternary Therapeutics, Dr Naail Kashif-Khan, CADD at Ternary Therapeutics.

To apply, or for more information visit this link.

[1+3] MRes + PhD Studentship for October 2026 - Targeting intractable cancer targets through universal proximity-induced pharmacology

Despite remarkable advances in medicine, cancer remains a leading cause of death worldwide. Many cancers still lack effective treatments, and numerous cancer-driving proteins remain undruggable by conventional small molecules. The recent emergence of proximity-induced therapeutics has created a unique opportunity to selectively eliminate such proteins through targeted degradation. This strategy harnesses the cell’s natural protein disposal machinery by recruiting E3 ubiquitin ligases using small-molecule drugs such as PROTACs or molecular glue degraders.

Although the human proteome encodes over six hundred E3 ligases, only a handful have been validated for use in targeted protein degradation (TPD), with Cereblon and Von Hippel–Lindau (VHL) being the most commonly exploited. While these E3s have enabled the degradation of more than a hundred targets, their activity is inherently limited, and many cancer-relevant proteins remain refractory to degradation. This highlights the urgent need to identify new E3 ligases suitable for TPD and to define the optimal binding sites that facilitate efficient ubiquitin transfer.

To address these challenges, we have developed a novel chemical biology platform termed Site-specific Ligand Incorporation-induced Proximity (SLIP). SLIP provides a universal and high-resolution approach to map ligandable sites on effector proteins by leveraging genetic code expansion (GCE) to incorporate unnatural amino acids (UAAs) at precisely defined positions. This enables systematic exploration of ligand–effector interactions with minimal structural perturbation. By focusing on ligandable cysteine residues and employing targeted covalent ligands, we will use SLIP-derived data to optimise induced-proximity kinetics, potency, and selectivity, thereby accelerating the design of next-generation therapeutics.

Supervisors: Professor Ed Tate, Department of Chemistry, Imperial, Dr Agnieszka Konopacka, ICR, Professor Dima Kozakov, The University of Texas at Austin.

To apply, or for more information visit this link.

Direct to PhD Studentships for October 2026 - Decoding mechanisms and drug targets in protein lipidation

Applications are invited for a 3.5-year PhD studentship in the Tate group at Imperial College’s White City Campus, on understanding mechanisms and identifying novel drug targets in protein lipidation post-translational modification (PTM). The specific focus of this project will be on enzymes modulating long-chain acylation at cysteine, known as S-acylation (or protein palmitoylation). Candidates will require a strong molecular sciences background at the Master level (e.g. MRes or MSci in chemistry, chemical biology, biochemistry, or molecular biology), and a passion for discovery science which can lead to therapeutic advances. Technologies we are currently applying to this challenge include enzyme/substrate engineering to enable discovery of S-acylation substrates in cells, chemical proteomics and interactomics, novel assay development for high-throughput screening and medicinal chemistry, encoded libraries (DELs, mRNA display), synthetic biology (DNA library design/selection), structure determination by cryoEM, genetic code expansion, and cell line engineering.

The studentship will be part of the EPSRC Centre for Doctoral Training in Chemical Biology: Empowering UK BioTech Innovation, at the Institute of Chemical Biology at Imperial, and is available to start in October 2026. Applicants must qualify for UK/Home fee status, and the successful candidate will receive an enhanced stipend of £10,000 above the UKRI minimum (total ca. £31,000 pa.) under the government’s  TechExpert pilot to help grow the UK’s national capability in chemical Biology and AI research, part of the UK’s modern industrial strategy. In return, you will take part in additional TechExpert activities for up to 10 days each year including outreach to promote tech careers, networking with the TechFirst community and engagement with the biotech industry.

Protein S-acylation is a rich and widespread class of protein post-translational modification (PTM), with key roles in signalling, cell death, immunity, protein stability and trafficking. More than 1000 proteins are S-acylated, including 150 cancer drug targets which are not amenable to traditional drug discovery. Intervening in the extensive network of enzymes regulating protein lipidation presents a unique opportunity to target these ‘undruggable’ proteins. The Tate lab has developed chemical proteomic technologies to study all the major classes of protein lipidation, including the first chemical genetic systems to map enzyme-specific S-acylation. We have also delivered target validation and novel lipidation inhibitors, co-founding Myricx Bio to translate our work to benefit patients. To date, Myricx has raised over $120  million, and will take our lipidation inhibitors into clinical trials in 2026, as first-in-class antibody-drug conjugate (ADC) payloads.

Supervisor: Professor Ed Tate, GSK Chair in Chemical Biology, Imperial College London and the Francis Crick Institute.

To apply, or for more information visit this link.

PhD studentships 

Any students interested in pursuing postgraduate research in our group other than the studentships listed above should contact Professor Tate directly; all prospective applicants should have or expect to obtain a 1st class honours degree (or equivalent) in chemistry, biochemistry, or a closely related discipline; non-UK students must be able to obtain independent funding for their studies, e.g. via a government bursary. 

Postdoctoral opportunities

We welcome informal enquiries from potential postdoctoral fellows with outstanding research track records who are prepared to apply for independent research funding, for example from the European Union, HFSP, etc. Full assistance will be given in preparing a competitive research proposal; we have an exceptional track record in accelerating the careers of outstanding postdoctoral researchers, with six Marie Curie fellows in our lab in the past four years.