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Welcome to the Hagan Bayley Lab
Chemical Research Laboratory | Department of Chemistry | University of Oxford

We are a chemical biology group which focuses on protein chemistry, molecular genetics and biophysics. Much of our work is centered on membrane proteins, in particular channels and pores. We are currently investigating both the fundamental properties of these proteins and their applications in biotechnology.

Several of our studies are collaborations with other laboratories in the UK, USA and Europe. There are currently 14 postdocs, 8 graduate students and a technician in the laboratory, from 12 different countries.
News from the Lab:
April 2014

  • OxSyBio raises £1 million to develop 3D printer. Our new spin-out company has raised £1 million from IP Group plc to advance the 3D droplet printing technology devised by the Bayley group. The technique involves printing synthetic tissue-like materials from thousands of tiny water droplets each coated in a thin film mimicking a living cell’s external membrane, and studding these membranes with protein pores so they act like simplified cells. OxSyBio will focus on the refinement of the technique for wound healing and drug delivery applications. In the longer term the company aims to print synthetic tissues for organ repair or replacement. The official press release from Isis Innovation provides more information on the announcement.
March 2014
  • Our research on using nanopores to detect protein modifications has been highlighted in Nature Methods.
February 2014
  • We welcome postdoc Linna Zhou, PhD students Jianfei Feng and Yujia Qing to the group!
  • We say goodbye to Visiting Prof. Lukas Tamm (Virginia, US) who was at Oxford on a 3 month sabbatical.
  • Our new paper entitled ‘Functional truncated membrane pores’ has been published in PNAS. The paper describes the development of a new class of membrane proteins that stabilise lipid pores, as toroidal structures.
January 2014
  • Our new paper entitled ‘Single-molecule site-specific detection of protein phosphorylation with a nanopore’ has been published in Nature Biotechnology. Using the model protein thioredoxin, we demonstrate the detection of site-specific phosphorylations. Analysis of the ionic current amplitude and noise, as the protein unfolds and moves through the αHL pore, enables distinction between unphosphorylated, mono- and di-phosphorylated variants.
  • Our new paper entitled ‘Detection of 3’-end RNA uridylation with a protein nanopore’ has been published in ACS Nano. Here, we demonstrate the detection of a post-transcriptional modification (uridylation) through studying the selective and transient binding of 3’-uridylated ssRNAs inside the beta-barrel of the αHL pore.

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