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Durham University

Biophysical Sciences Institute

Biophysical Sciences Institute

"The BSI is a community of interdisciplinary academics, researchers and students who have research interests at the boundary between the life sciences and the other sciences including physics, chemistry and psychology, as well as mathematics and engineering."

- Associate Professor Steven Cobb, BSI Director.

Honorary Doctor of Science awarded to BSI Advisory Group member

Congratulations! to Dr Elspeth Garman, Oxford Univerity, who was awarded an honorary Doctor of Science, at Durham University Summer Congregation 2019.

As well as being a Visiting Professor within the Chemistry department Elspeth is a member of the BSI Advisory Group, and we join our colleagues in congratulating her on this well-deserved recognition of her research and work within the world of Biophysics.

Discovery of Paradoxical Geometries published in Nature

An international group of researchers from the Jagiellonian University (Krakow, Poland), led by Prof J. Heddle, have produced a super-stable artificial protein ball that apparently defies the rules of geometry. The nano-cage is made out of 24 regular hendecagons (polygons with 11 edges) but this is known to be mathematically impossible. Bernard Piette (Department of Mathematical Sciences, Durham University) and visiting PhD Student Agnieszka Kowalczyk (Department of Mathematics and Malopolska Centre of Biotechnology, Jagiellonian University) have shown that the shape realised in the lab is possible if one distorts the edges and the angles of the polygons by 0.5% and 0.27% respectively. They have also identified several other, so called, paradoxical geometries by defining cages with are made out of nearly regular polygons as well as some, less regular, holes.

Beside their mathematical interest, these geometries are candidates to create artificial proteins cages which can be used for drug delivery. The drug is trapped inside protein cages which are themselves dressed with ligands that can bind to the receptors of target cells, like a cancer cells for example. The advantage is to reduce side effects as the drug is only delivered to the cells that needs to be. This can also lead to reduced cost, especially for very expensive drugs, as smaller amounts of the chemical are needed.

Protein cages exists in nature, as viruses for example, but the advantage of the protein cage made by the Heddle lab is that is is made of a single protein. In nature the many proteins that form a protein cage are held together by a complex network of chemical bonds and these are very difficult to predict and simulate. This makes engineering new cages of that type very difficult. The cage created by the Heddle Lab, on the other hand, is made out of a single protein that forms so called rings, the polygonal faces of the cage. These rings are then linked together by gold atoms to form a cage with a 22nm diameter. The identification of other paradoxical geometries, as found by Bernard Piette and Agnieszka Kowalczyk, will help bio-chemists to select proteins which can form "rings" from which other types of cages can be made.

The research has been published in Nature which can be accessed from http://dx.doi.org/10.1038/s41586-019-1185-4 or https://rdcu.be/bATfi

Interestingly, Jonathan Heddle, who led the discovery, is originally from Bishop Auckland and is a regular visitor of the Department of the Mathematical Sciences Department and the Biophysical Science Institute in Durham.


Figure 1. An electron density representation of the "mathematically impossible" protein cage, around 22 nanometres in diameter. The cage is made from 24 copies of an 11-sided, ring-shaped protein each shown in a different colour and held together by single gold atoms (yellow balls). The background shows models of other "Impossible" cages predicted by the work. Image attribution: Heddle Lab, Jagiellonian University

EPSRC CDT in Molecular Sciences for Medicine

Congratulations to BSI Co-Director Ehmke Pohl, BSI Director Steven Cobb, and BSI member Paul Denny who have, alongside their Newcastle collegues, secured over £5m of CDT funding from the Engineering and Physical Science Research Council, to be used to train 60 PhD students over the next 9 years in Molecular Sciences for Medicine.

The programme will draw upon Durham's physical science expertise and Newcastle's biomedical approach and students will be supported by a strong network of industry partners and experts both regionally and internationally.

Further information can be found on the Chemistry press release, and at the MosMed website