The structure of a protein is vital in its ability to function correctly in the human body. It has been well documented that protein misfolding can result in the formation of stable aggregates which are typically associated with increased amounts of �-sheet and can lead to a diseased state. However, in the model peptide Poly-L-lysine, PLL, the formation of �-sheets can be reversible.  Here, the kinetics of the protein folding pathway of PLL at various pH and temperatures were studied using infrared spectroscopy.  It was observed that PLL forms a-helices rapidly upon dissolution at basic pH; over time, it refolds to form �-sheets. Surprisingly, further incubation of PLL causes the disaggregation of �-sheets into a random configuration.  The time PLL spends in each conformational state is dependent on pH and temperature. These studies provide insight into the mechanism of disaggregation, which could be exploited to recover function in misfolded proteins.

Mapping the energy landscape of a model peptide using infrared spectroscopy

243rd National Meeting (2012)

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