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Details of Grant 

EPSRC Reference: GR/S98375/01
Title: The physics of aggregation of the protien beta lactoglobulin (BLG)
Principal Investigator: Donald DBE FRS, Professor A
Other Investigators:
Researcher Co-Investigators:
Project Partners:
Department: Physics
Organisation: University of Cambridge
Scheme: Standard Research (Pre-FEC)
Starts: 01 August 2004 Ends: 31 March 2008 Value (£): 300,467
EPSRC Research Topic Classifications:
Chemical Biology Complex fluids & soft solids
Materials Characterisation
EPSRC Industrial Sector Classifications:
Food and Drink Healthcare
Related Grants:
Panel History:  
Summary on Grant Application Form
Beta lactoglobulin is a very common protein found in milk. Its gels are widely used in the food industry, but nevertheless many facets of its aggregation are not well understood. Two classes of gels can be identified: around its isolectric point of pH 5.13 particulate gels form, whereas well away from this pH in both acidic and alkaline conditions, fibrillar gels form. These fibrils have recently been identified with amyloid fibrils, now recognized as underlying a wide variety of diseases and whose importance is increasingly recognized. This project aims to study the pathways of aggregation in both regimes. In addition, larger scale aggregates also form in the fibrillar gels giving rise to structures reminiscent of spherulites under the polarising microscope. Conditions which promote spherulitic formation will also be explored. Key factors to be studied throughout will be the relative importance of kinetics versus thermodynamic equilibrium, and the importance of charge. In addition, throughout the project the specifics of the BLG behaviour will be put in the context of the broader picture of the behaviour of other proteins.
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Organisation Website: http://www.cam.ac.uk