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Melbourne School of Engineering
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Peter AsimakisPost Graduate Complex Fluids Group
Department of Chemical & Biomolecular Engineering
Room 2.27, Second Floor, Building 165
The University of Melbourne
Victoria 3010 Australia
Email: asip@unimelb.edu.au Tel: (03) 8344 4888 Fax: (03) 8344 4153 Parkville Campus Map
Current Research Activities “Protein Aggregation during Processing”
Protein aggregation is a common issue during the processing of food and biotherapeutics. The term aggregation is usually used to describe the type of interaction or characteristic of a protein solution. Aggregation of proteins can be soluble or insoluble. Insoluble particles are usually removed by filtration. However, soluble aggregates are typically small and difficult to remove. Proteins are exposed to various conditions during manufacture and formulation of therapeutic products. Conditions such as temperature, pH, and shear reduce the stability of proteins, leading to loss of structure through conformational change. This loss of structure often presents as aggregation. The presence of aggregates in final therapeutic products is undesirable as it may result in an increased rate of adverse reaction and higher immunogenicity. This project aims to investigate the effect processing has on the stability of therapeutic proteins. A series of controlled experiments will expose the protein solutions to various temperatures, pH values, and shear rates. These experiments will be used to determine the mechanism of aggregate formation. Our hypothesis is that these aggregate species may follow an amyloidogenic pathway, becoming highly ordered and forming amyloid fibrils. Amyloid fibrils are associated with many conformational diseases such Alzheimer’s and Parkinson’s disease.
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Date Created: 29 April 2004 |
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