Louise Farmer Makes it Three Out of Three for Leicester!

Congratulations to Louise Farmer who has won the 2013 East Midlands Engineering and Science Professionals Prize.

Louise FarmerBeating off strong competition from entrants from other East Midlands universities, Louise won for her presentation on her research into the P2X1 receptor - work which could eventually lead to new treatments for blood clots that could save lives and over £300 million in costs to the NHS each year.

Louise's win makes it three in a row for Leicester following wins in this competition by Andrew Vanezis in 2012 and Will Nicholson in 2011.

About Louise Farmer 

Louise Farmer is a research student in the Department of Cell Physiology and Pharmacology. Her studentship is sponsored by the British Heart Foundation. Louise is currently working towards completion of her doctoral thesis and is supervised by Professor Richard Evans

Originally from Essex, Louise moved to Leicester in 2007 to undertake a BSc in Medical Physiology and it was in the third year of that degree that Louise first worked on P2X receptors. Having enjoyed this work and the techniques involved, Louise stayed on at Leicester for her doctoral degree.

Her results have been presented at conferences in the UK and internationally.

About Louise's Research - Blood Clotting: A Study on the P2X1 Receptor

Blood clotting is a vitally important process. When an individual is wounded, clotting and scab formation occur in order to prevent further blood loss and to avoid infection. However this can go wrong when clots, or thrombi, form inside blood vessels. A thrombus can become dangerous if it occludes the vessel, or if a piece of the clot breaks free, enters the blood stream and creates a blockage elsewhere, called an embolism. If this occurs the delivery of oxygen to tissues is prevented and can lead to various conditions. It has been estimated that the treatment of embolisms costs the NHS £640 million a year. This figure is particularly high when you take into consideration that current treatment is far from ideal. The most commonly prescribed drug is the anticoagulant Warfarin, which was originally developed as a rat poison. There are approximately 950,000 people taking Warfarin in the UK. Whilst making embolisms less likely, the drug also decreases the speed at which scabs form and makes patients prone to bleeding and bruising. Even minor injuries can have serious consequences. It is estimated that the NHS spends an estimated £8.5 million a year treating patients on Warfarin who have haemorrhages. Due to these side effects monitoring of patients on the drug costs the NHS further, an estimated £383 per patient per year. This totals £383 million, a significant proportion of the cost of managing embolisms. From these statistics it is clear that not only would a more effective drug with fewer side effects greatly benefit patients, but it would save the NHS millions of pounds.

The ideal anticoagulant drug would prevent clots occurring in blood vessels but still allow the formation of a scab if a patient were to injure themselves. There is a protein called P2X1 that was genetically removed from mice in a previous study. These mice showed a decrease in thrombi in vessels but there was no effect on wound clotting. This is the ideal scenario for an anticoagulant. If a drug could stop the P2X1 protein working then it could be a much better anticoagulant than Warfarin. All drugs have a binding site on their target protein. The drug needs to be designed so that it fits tightly to this binding site. If the drug is not specific enough to its particular site then it will also affect other proteins, causing unwanted side effects. There is a drug that blocks P2X1. However it is not specific and cannot be used therapeutically due to its side effects. If the binding site of the existing drug on P2X1 can be identified, a new drug can be designed that is a more specific fit for the protein and could be used therapeutically. The aim of my project was therefore to identify the location of the P2X1 inhibitor binding site.

To do this I have used another protein, which is related to P2X1, called P2X4. The inhibitor cannot interact with this receptor, as the binding site for the drug is not present. Using cutting-edge molecular biology techniques, similar to those used in the pharmaceutical industry, I have replaced sections of P2X1 with corresponding regions of P2X4 in a series of chimeras. If the drug no longer prevents P2X1 activation then it can be assumed that a section of the binding site has been removed. By making over 60 chimeras I have identified the probable binding site of the drug. This can now be used in intelligent drug design to make a new anticoagulant, specific to P2X1.

Compared to Warfarin, development of the new P2X1 based anticoagulant could save the NHS £363 million a year in monitoring costs and an estimated £8.5 million in treating Warfarin patients who haemorrhage. As it would not make patients prone to bleeding, it could also be taken in patients with high risk of clot formation before an event were to occur. This would reduce the number of people having embolisms, saving the NHS a significant proportion of the £640 million it spends on treatment each year. It would also have a huge benefit to the lives of patients, as it would remove the need to routinely return to hospital for monitoring and they would not have to live their lives in fear of injury. In conclusion, a P2X1 targeted anticoagulant would be hugely beneficial, both socially and economically.

About East Midlands Engineering and Science Professionals

East Midlands Engineering and Science Professionals provides a voice on the common issues for the engineering and science profession in the East Midlands and works to make people more aware of the vital contribution that engineering and science make to the economy, prosperity, and quality of life in the region.

The EMESP Prize is an annual award given to a postgraduate researcher from one of the region's universities. In 2011, 2012, and 2013 the EMESP Prize has been won by the University of Leicester. 

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