Emma Shardlow - Keele University
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Bioinorganic Chemistry of Aluminium & Silicon

Emma Shardlow

Emma Shardlow I graduated from Keele University in July 2011 with 1st class honours in Biochemistry and Medicinal Chemistry.

During the final year of my undergraduate degree I undertook an experimental project under the supervision of Dr Chris Exley (now Prof.) which aimed to investigate how Cu2+ ions, introduced at a variety of concentrations, influenced the formation of ProIAPP1-48 amyloid in vitro both solely and in the presence of other ions such as Al3+ and Zn2+. ProIAPP1-48 amyloid deposition within pancreatic beta cells is a common pathological feature of non-insulin dependent Diabetes Mellitus (NIDDM). Cu2+ ions have been shown to abolish ProIAPP1-48 amyloid formation in vitro, but only at high concentrations (320μM) (Exley et al., 2010). Our results demonstrated that Cu2+ ions at concentrations as low as (10μM) prevented and abolished ProIAPP1-48 amyloid formation in vitro illustrating the therapeutic capacity of Cu2+ ions to reduce NIDDM associated amyloidogenicity.

After spending a brief spell in industry, analysing samples within a microbiology laboratory, I returned to Keele in September 2011 and am currently undertaking a PhD under the supervision of Prof. Chris Exley studying the bioinorganic chemistry of Aluminium-based adjuvants. Adjuvants are the immunopotentiating components of a vaccine solution i.e they enhance the immune response to the small concentration of co-administered antigen. Despite the current widespread use of aluminium adjuvants within human vaccinations, the mechanisms by which they promote an immune response in vivo remain unclear. Therefore, the main aim of this project is to determine the biological availability and mechanistic actions of aluminium-based adjuvants used in human vaccines.

At present I am researching the physiochemical aspects of clinically approved adjuvant materials using a variety of analytical techniques in order to gain a greater understanding of their content and structure.

References

Exley, C. House, E. Patel, T. Wu, L. Fraser, P. E. (2010) Human pro-islet amyloid polypeptide (ProIAPP1-48) forms amyloid fibrils and amyloid spherulites in vitro. Journal of Inorganic Biochemistry. 104(10): 1125-1129