BH3 helix-derived biophotonic nanoswitches regulate cytochrome c release in permeabilised cells.
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.
School of Chemistry, Cardiff University, Main Building, Park Place, Cardiff CF10 3AT, UK. allemannrk@cardiff.ac.uk.
Robert J
RJ
Mart
Rachel J
RJ
Errington
Catherine L
CL
Watkins
Sally C
SC
Chappell
Marie
M
Wiltshire
Arwyn T
AT
Jones
Paul J
PJ
Smith
Rudolf K
RK
Allemann
D000478:Alkylation / Q000187:drug effects; D000595:Amino Acid Sequence; D001391:Azo Compounds / Q000737:chemistry / Q000494:pharmacology; D045744:Cell Line, Tumor; D045304:Cytochromes c / Q000378:metabolism*; D006801:Humans; D008928:Mitochondria / Q000187:drug effects / Q000378:metabolism; D010446:Peptide Fragments / Q000737:chemistry / Q000494:pharmacology*; D017433:Protein Structure, Secondary; D011518:Proto-Oncogene Proteins / Q000737:chemistry / Q000494:pharmacology*
D001391:Azo Compounds; C474007:Bax protein (53-86); D010446:Peptide Fragments; D011518:Proto-Oncogene Proteins; D045304:Cytochromes c; C009850:azobenzene