Austerberry, James, Miller, Aline and Belton, Daniel J. (2010) Elucidating the mechanism and thermodynamics of protein aggregation in order to create novel biomaterials. In: Nanoformulation 2010, 9th – 11th June 2010, Stockholm, Sweden. (Unpublished)

Protein aggregation occurs under certain conditions that cause individual protein sub-units to adhere to one another. Such conditions include extreme pH, high salinity and elevated temperatures. Understanding protein aggregation is important for many areas, including the improvement of processing and formulation of biopharmaceuticals, elucidating the mechanism of neurodegenerative diseases and manufacturing novel biomaterials. The morphology of protein aggregates can be controlled by tuning the environmental conditions that cause the proteins to adhere to one another, leading to the formation of fibrils, spherulites or particulates, which in turn can aggregate to form higher order structures. The ability to control aggregate morphology allows the potential to create novel architectures for new functional materials, such as complex tissue scaffolds, drug delivery systems, nano meshes and more. However, the mechanism and thermodynamics for protein aggregation is not fully understood. Here, we present results from light scattering and microscopy for several model protein systems which have been subjected to conditions that induce the formation of particulate aggregates. This has allowed the formation and structure of these aggregates to be examined in detail, which in turn has led to a better understanding of the mechanism and thermodynamics for their formation. Overall, the work gives us important insights into protein aggregation, which will eventually allow us to control and adapt this process in order to derive a range of benefits.

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