Production of Distinct Fibrillar, Oligomeric, and Other Aggregation States from Network Models of Multibody Interaction

Elizabeth M. Diessner, Loring J. Thomas, and Carter T Butts

Journal of Chemical Theory and Computation

Protein aggregation can produce a wide range of states, ranging from the fibrillar structures and structured oligomers implicated in diseases such as Alzheimer's and Lewy Body Dementia to unstructured and semistructured gel phases.   How protein sequence and solution conditions conspire to produce this diversity of states is still poorly understood. In this paper, we use a family of network-based models to show how distinct aggregation phases arise from the balance of forces affecting multi-body interactions among protein monomers.  Our model suggests that the relative strength of factors affecting branching, elongation, and cyclization determine phase boundaries, providing general insights into when and why potentially toxic species may be likely to form.

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