Davies, Hannah - University of Liverpool - Department of Biochemistry

个人简介

I obtained a BSc (Hons) in Biochemistry and then a PhD from the University of Liverpool. My PhD thesis was entitled 'Expression and characterisation of cardiovascular amyloid proteins'. This work was centred around a small amyloidogenic protein called medin found in the aorta. Medin amyloid is the most common form of localised amyloid and is found in 97% of the population over 50 however very little is known about the role of these amyloid plaques in the aorta. My PhD work was focussed on developing methods to recombinantly produce medin and then study the aggregation properties and structure of this small protein. I am now working as a research associate on a grant funded by the British Heart foundation. This grant has expanded upon my PhD work with medin to include study of many additional cardiovascular amyloid proteins. I am particularly interested in the interaction of different amyloid proteins and the consequences in disease. Travel award to attend the XIVth International Symposium on amyloidosis (Prize, International society of amyloidosis organising committee 2014) Research seminar (Invitation to Speak, National institutes for Health, USA 2014) Excellence in Innovation award (Prize, University of Liverpool Celebrating success awards 2012) Travel award to attend the XIIIth International Symposium on amyloidosis (Prize, International society of amyloidosis organising comittee 2012) Research seminar (Invitation to Speak, Nuclear magnetic resonance discussion group (NMRDG) 2010) Poster prize (Prize, Nuclear magnetic resonance discussion group (NMRDG) 2010)

近期论文

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HUMAN MICROVASCULAR ENDOTHELIAL DYSFUNCTION INDUCED BY AMYLOIDOGENIC MEDIN PROTEIN Comparisons with Amyloid-beta Reveal an Aspartate Residue That Stabilizes Fibrils of the Aortic Amyloid Peptide Medin. H-1, N-15 and C-13 assignment of the amyloidogenic protein medin using fast-pulsing NMR techniques Nanoliposomes protect against human arteriole endothelial dysfunction induced by beta-amyloid peptide. Oxidative Stress Alters the Morphology and Toxicity of Aortic Medial Amyloid. Expression and purification of the aortic amyloid polypeptide medin. Fibrils and nanotubes assembled from a modified amyloid-beta peptide fragment differ in the packing of the same beta-sheet building blocks. Solid state NMR reveals differences in the packing arrangements of peptide aggregates derived from the aortic polypeptide medin. Expression and characterisation of cardiovascular amyloid proteins