Matthew Mold - Keele University
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Bioinorganic Chemistry of Aluminium & Silicon

Matthew Mold - Post-doctoral Research Assistant

Matthew Mold

Background

In 2008 I graduated from Staffordshire University with 1st class honours in BSc Forensic Science.

In the third and final year of my degree I undertook a dissertation with the title, "False Positives in the Presumptive Testing of Cocaine". The study involved analysing a range of chemicals (from local anaesthetics to common household substances), in the identification of false positives; to establish the most sensitive and selective tests when identifying cocaine recovered from crime scenes. The final outcome of the project was the development of a bench top method for the quantification of cocaine without the need for sample pre-treatment by modifying the protocols of a cobalt thiocyanate based test.

I am now in the final stages of completing my PhD thesis with the title, “Complementary studies of the role of metals in the conformation and interactions of serum amyloid P component and β-amyloid Aβ42”. Amyloidogenic peptides have frequently been implemented in the causation of neurodegenerative diseases, and my thesis involves studying the effects of varying chemical environments on the self-aggregating propensities of amyloid.

Current Research

I have recently started a post-doctoral research associate (PDRA) position working with Prof. Christopher Exley and his group, on the nanotoxicity of Aluminium adjuvants. The post has been generously funded by the Medical Research Council (MRC) for three years.

Publications

  1. EXLEY, C., MOLD, M., SHARDLOW, E., SHUKER, B., IKPE, B., WU, L. & FRASER, E. P. 2012. Copper is a potent inhibitor of the propensity for human ProIAPP 1-48 to form amyloid fibrils in vitro. Journal of Diabetes Research & Clinical Metabolism, 1.
  2. HOUSE, E., MOLD, M., COLLINGWOOD, J., BALDWIN, A., GOODWIN, S. & EXLEY, C. 2009. Copper Abolishes the beta-Sheet Secondary Structure of Preformed Amyloid Fibrils of Amyloid-beta(42). Journal of Alzheimer's Disease, 18, 811-817.
  3. MOLD, M., SHRIVE, A. K. & EXLEY, C. 2012. Serum Amyloid P Component Accelerates the Formation and Enhances the Stability of Amyloid Fibrils in a Physiologically Significant Under-Saturated Solution of Amyloid-beta(42). Journal of Alzheimers Disease, 29, 875-881.
  4. MOLD, M., OURO-GNAO, L., WIECKOWSKI, B., & EXLEY, C. 2013. Copper prevents amyloid-beta(1-42) from forming amyloid fibrils under near-physiological conditions in vitro. Nature Scientific Reports, 3, article no. 1256, DOI:10.1038/srep01256.

Contact Details

LJ 0.04B,
Birchall Centre,
Lennard-Jones Laboratories,
Keele University,
Staffordshire, ST5 5BG, UK.

Email: m.j.mold@keele.ac.uk

T: 01782 733508