Membrane fusion is one of the key events in many cellular processes and is often assisted or necessitated by membrane fusion proteins, which often contain a membrane interacting domain or a fusion peptide. While fusion peptides have been the subject of many previous studies, their mechanism of action is still not well understood. Herein, using the influenza hemagglutinin fusion peptide (HAfp) as a model, we show how stopped-flow fluorescence, FRET, and pH-jump techniques and global data analysis can be combined to dissect various molecular events underlying peptide-membrane interactions in general and to specifically provide new insights into the folding mechanism of HAfp.

Kinetic measurements provide new insights into the folding mechanism of a fusion peptide and its interaction with membranes

245th National Meeting (2013)

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