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A Kinetic Study of Ovalbumin Fibril Formation: The Importance of Fragmentation and End-Joining

2015; Elsevier BV; Volume: 108; Issue: 9 Linguagem: Inglês

10.1016/j.bpj.2015.03.021

1542-0086

Jason M. D. Kalapothakis, Ryan J. Morris, Juraj Szavits-Nossan, Kym Eden, Sam Covill, Sean Tabor, Jay Gillam, Perdita E. Barran, Rosalind J. Allen, Cait E. MacPhee,

Protein Structure and Dynamics

The ability to control the morphologies of biomolecular aggregates is a central objective in the study of self-assembly processes. The development of predictive models offers the surest route for gaining such control. Under the right conditions, proteins will self-assemble into fibers that may rearrange themselves even further to form diverse structures, including the formation of closed loops. In this study, chicken egg white ovalbumin is used as a model for the study of fibril loops. By monitoring the kinetics of self-assembly, we demonstrate that loop formation is a consequence of end-to-end association between protein fibrils. A model of fibril formation kinetics, including end-joining, is developed and solved, showing that end-joining has a distinct effect on the growth of fibrillar mass density (which can be measured experimentally), establishing a link between self-assembly kinetics and the underlying growth mechanism. These results will enable experimentalists to infer fibrillar morphologies from an appropriate analysis of self-assembly kinetic data.