Dr Philip Kitchen

Supervisor Details

Contact Details

Scientific Background

Research Interests

My research interests are focused on the study of membrane proteins, spanning from single molecule studies to advanced tissue engineering. Current projects in the lab include developing iPSC-based models of the human blood-brain barrier, drug discovery for brain oedema by inhibiting aquaporin channel function or localisation, characterising the interactome of various membrane proteins, using mass photometry to characterise membrane protein oligomerisation, optimising solubilisation conditions for G protein-coupled receptors, and cryo-EM studies of aquaporins using novel membrane solubilising agents.

Supervision Style

In three words or phrases: Laid-back, spontaneous, and collaborative.

Provision of Training

I prefer to take responsibility for your technical training at first, leading to more independence later. I am a research fellow on a research-only contact, so my minimal undergraduate teaching responsibilities mean that I have plenty of time to work with students in the lab.

Progression Monitoring and Management

I meet students weekly to discuss results, experimental plans, and methodology.

Communication

We will communicate primarily by email; you would not be expected to check emails outside of normal working hours. The team also has a WhatsApp group chat with which we regularly communicate during the week and weekends. As I currently spend most of my time in the lab, communication may also be on a more informal ad hoc face-to-face basis.

PhD Students can expect scheduled meetings with me:

In a group meeting

At least once a week

In year 1 of PhD study

At least once a week

In year 2 of PhD study

At least once a week

In year 3 of PhD study

At least once a week

These meetings will mainly be face to face, and I am usually contactable for an instant response on every working day.

Working Pattern

The timing of work in my lab is completely flexible, and (other than attending pre-arranged meetings), I expect students to manage their own time.

Notice Period for Feedback

I need at least 1 week’s notice to provide feedback on written work of up to 5000 words.

MIBTP Project Details

Current Projects (2025-26)

Primary supervisor for:

Cryo-EM studies of SMA-solubilised membrane proteins

See the PhD Opportunities section to see if this project is currently open for applications via MIBTP.

Please Note: The main page lists projects via BBSRC Research Theme(s) quoted and then relevant Topic(s).

Cryo-EM studies of SMA-solubilised membrane proteins

Secondary Supervisor(s): Dr Emma Hesketh (Leicester), Professor Roslyn Bill

University of Registration: Aston University

BBSRC Research Themes:

Renewable Resources and Clean Growth (Industrial Biotechnology)
Understanding the Rules of Life (Neuroscience and Behaviour, Structural Biology)

Project Outline

Membrane proteins are crucial for life, providing the basis for cells to sense and interact with their environment. They are also very important for drug discovery – despite only making up around 25–30% of the human proteome, they account for over 60% of therapeutic drug targets.

As membrane proteins are generally hydrophobic, solubilising agents are required to remove these proteins from the complex environment of a biological membrane and keep them in solution for further study. Traditionally, this has been done using detergents, amphipathic molecules that form micelles around membrane proteins to solubilise them. However, there are key weaknesses with this approach, including instability/denaturation of the protein, the need to screen a variety of detergents to find the optimal detergent for a specific protein, and the loss of protein-lipid interactions which could be crucial for protein structure and/or function. As a result, membrane protein researchers have explored alternatives to detergents. One of these alternatives is styrene maleic acid (SMA) polymers. SMA inserts into membranes and forms small discs of membrane encapsulated by the polymer. Membrane proteins solubilised in this way retain an annulus of lipids from the host cell membrane, and have improved thermal stability compared to detergent-solubilised membrane proteins (Unger et al, 2021, doi:10.1042/BST20201067).

In recent years, advances in electron microscopy hardware and image processing techniques have led to the ‘cryo-EM resolution revolution’, making it possible to solve protein structures at near-atomic resolution using cryo-EM. There is now an opportunity to combine these two transformative technologies to study the structural biology of membrane proteins.

This project will investigate the use of SMA for membrane protein structural biology using cryo-EM. Initial focus will be on proteins currently of interest to the newly-established Aston Institute of Membrane Excellence (AIME), including aquaporin water channel proteins, G protein-coupled receptors, and ATP-binding cassette transporters. However, we are keen to work with a range of membrane proteins, and the student will be encouraged to work on further proteins that match their own scientific interests.

Co-supervisor on a project with Dr Grant Pellowe.