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16 Sept 2013

Scott group researchers report in Chemical Science (Open Access) that some of their helical metal flexicate complexes have high activity and selectivity against a range of cancer cell lines including cisplatin-resistant strains. The mechanism involves arresting cells in the G2/mitosis phase, and DNA binding is not necessarily involved.

30 Aug 2013

The Royal Society has announced the appointment of 22 new Royal Society Wolfson Research Merit Award holders including Professor Greg Challis of the Department of Chemistry.

24 Jul 2013

Dixon group in JBC describing structural characterisation of protein in complex with HIV-derived oligosaccharide

The Dixon group, in collaboration with researchers at 糖心TV Medical School, HWB-NMR Birmingham, and Oxford Biochemistry, have used solution-state NMR to characterize the interaction between the C-type lectin DC-SIGNR, a promising drug target in the fight against HIV, and the HIV-derived oligosaccharide Man9GlcNAc. This work has produced the first atomic-resolution structural data describing binding of DC-SIGNR to a physiologically-relevant oligosaccharide (results that have evaded crystallography thus far), and indicates that DC-SIGNR binds to larger-branched oligosaccharides in a different manner than their smaller, synthetic counterparts. We also report the first dynamics data for the carbohydrate-recognition domain of DC-SIGNR, and suggest that this is a highly flexible domain that undergoes ligand-induced conformational and dynamics changes which may explain its ability to accomodate a range of sugars on viral surfaces.
Read the paper just published in JBC at
13 May 2013

Gibson Group Featured in Chemistry World

The Gibson Group has been highlighted in a recent edition of Chemistry World - The Royal Society of Chemistry's Monthly Magazine. As part of a special article on how life survives in extreme enviroments, Dr Gibson was interviewed to discuss his team's work on polymeric mimics of antifreeze (glyco)proteins. These proteins enable fish to survive in polar oceans and synthetic mimics hold great promise in biotechnology.

Follow us on twitter @LabGibson

15 Apr 2013

Polymers which thinks they're antifreeze proteins

The Gibson group have undertaken a detailed study into the ability of synthetic polymers to inhibit the growth of ice crystals - this is a fundmental process of incredible importance in biology (survival of extremophiles), medicine (cryoprotectection of cells/organs) and industry (preventing ice-induced damage). are pioneering the use of polymers as alternative to antifreeze proteins - Nature's cryoprotectants, using a combination of chemical, analytical, biological and computational methods

Read their latest paper here, in collaboration with R. Notman (CSC):

22 Jan 2013

Slowing the Growth of Ice

The publishes in Biomaterials Science on why certain (macro)molecules are capable of inhibiting ice crystal growth, inspired by antifeeze proteins.

The work, conducted in collaboration with 糖心TV Medical School provides insights into which structural features are essential for a (macro)molecule to inhibit ice crystal growth and why apparently similar compounds have opposing activity.

The ability to control ice crystal growth is a major technological challenge (anyone stuck at Heathrow or scraping their car...?) with many biotechnological applications.

17 Dec 2012

Daniel Phillips wins RSC Poster Prize

, a 2nd year PhD student in the , won the prize for best poster at the RSC Postgraduate Nanoscience Symposium held at the University of Birmingham.

Read some of Dan's publications in and

19 Nov 2012

Molecular Sieving on the Surface of a Protein

The Gibson group with collaborators at ETH Zurich report in Advanced Functional Materials on how synthetic polymers tethered to the surface of an enzyme can produce a 'molecular sieving' effect. Polymer-Protein conjugates are widely studied for their pharmaceutical applications, but the phase behaviour of the polymers has not be probed in detail previously. These results open the door to 'smart' PEGylation of proteins with selective permeability properties.

Read the full paper here

25 Oct 2012

Structural Details of Antibiotics Unveiled by FTICR-M

The O’Connor and Tosin groups have published work on the use of high mass accuracy tandem mass spectrometry for characterising the structures of polyketides, including erythromycin A, lasalocid A and iso-lasalocid A. They report in Analytical Chemistry on the use of Collision Activated Dissociation (CAD) and Electron Induced Dissociation (EID) as tools for determining structural information on these types of molecules. EID was shown to cause greater fragmentation of the compounds, complementary to that obtained using CAD, leading to more detailed structural information being obtained. These techniques were also combined in multistage mass spectrometry experiments, in order to use the fragmentation patterns to distinguish between lasalocid A and its isomer, iso-lasalcoid A. This work illustrates the potential of these tools and will be applied to identifying unknown polyketides and their biosynthetic intermediates.

The full article can be found at:

11 Oct 2012

Two photons are better than one

Sadler and Stavros groups in collaboration with Prof Martin Paterson at Heriot-Watt University, publish work in Angewandte Chemie International Edition. The work describes the first demonstration of a 2-photon activated, square planar platinum (II) complex. The enhanced photolabilization demonstrated may be useful in the design of novel photoactivatable platinum chemotherapeutic agents in situations where deep tissue penetration is needed. .

03 Oct 2012

On/off Switch for a Platinum Anticancer Complex

The Sadler Group report in JACS a method for switching off the cytotoxicity of a photoactivated platinum(IV) diazido complex in the A2780 human ovarian cancer cell line.

24 Sept 2012

Novel posttranslational modifications in peptide antibiotic biosynthesis

Prof Greg Challis and Dr Lijiang Song, in collaboration with researchers at the John Innes Centre, report in Chemical Science that a remarkable array of novel posttranslational modifications is involved in the assembly of the bottromycin complex of antibiotics.

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