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The chemical and physical factors driving the self assembly of proteins - Jennifer McManus

Maynooth University


The chemical and physical factors driving the self assembly of proteins

Jennifer McManus, Maynooth University

The ability to control the self-assembly of biological molecules to form defined or functional structures with a high degree of predictability is a central aim for soft matter science and synthetic biology. While this is possible for a variety of colloidal materials, it has been more difficult to achieve for proteins. In large part, this is due to the complex chemical nature of the protein surface, which influences the assembly process. It is therefore important to understand this complexity to reveal the mechanisms underlying important processes such as protein crystallization, the pathogenesis of protein condensation diseases, the aggregation of proteins during industrial manufacture and the formation of protein based materials. Recent results probing the extent to which protein surface anisotropic interactions influence protein self-assembly will be presented. Using phase diagrams for human gamma D crystallin (a protein found in the human eye lens), both mutagenesis and chemical modification of the protein surface are used to probe the affect of altering the protein surface chemistry. We will demonstrate the even small change to the protein surface can dramatically affect its phase behavior. We will also present recent work on the formation of bigels by spinodal decomposition of unfolded protein to form a new type of protein hydrogel with enhanced mechanical properties. These double network materials, comprised of two discrete but interpenetrating networks are formed under controlled conditions to ensure minimal inter-species interactions during the self-assembly process.

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