Dynamic physical interactions between proteins underpin all key cellular processes and are a highly attractive area for the development of research tools and medicines. Protein-protein interactions frequently involve α-helical structures, but peptides matching the sequences of these structures usually do not fold correctly in isolation. Therefore, much research has focused on the creation of small peptides that adopt stable α-helical structures even in the absence of their intended protein targets. We show that short peptides alkylated with azobenzene crosslinkers can be used to photo-stimulate mitochondrial membrane depolarization and cytochrome c release in permeabilised cells, the initial events of the intrinsic apoptosis pathway. © 2013 The Royal Society of Chemistry.
CITATION STYLE
Mart, R. J., Errington, R. J., Watkins, C. L., Chappell, S. C., Wiltshire, M., Jones, A. T., … Allemann, R. K. (2013). BH3 helix-derived biophotonic nanoswitches regulate cytochrome c release in permeabilised cells. Molecular BioSystems, 9(11), 2597–2603. https://doi.org/10.1039/c3mb70246d
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