Journal
CHEMISTRY & BIOLOGY
Volume 17, Issue 7, Pages 735-744Publisher
CELL PRESS
DOI: 10.1016/j.chembiol.2010.05.018
Keywords
-
Categories
Funding
- Samantha Dickson Brain Tumour Trust
- Swedish Research Council (VR-NT)
- Center for Biomembrane Research, Stockholm
- Knut and Alice Wallenberg's Foundation
- EU through Center of Excellence in Chemical Biology, Estonia
- Estonian Government [SF0180027s08]
- DoRa Program
- Archimedes Foundation
Ask authors/readers for more resources
Cell penetrating peptides (CPPs) with intrinsic biological activities offer a novel strategy for the modulation of intracellular events. QSAR analysis identified CPPs within human cytochrome C. Two such sequences, Cyt c(77-101) and Cyt c(86-101), induced tumor cell apoptosis, thus mimicking the role of Cyt c as a key regulator of programmed cell death. Quantitative analyses confirmed that Cyt c(77-101) is an extremely efficient CPP. Thus, Cyt c(77-101) was selected for modification to incorporate target-specific peptidyl motifs. Chimeric N-terminal extension with a target mimetic of FG nucleoporins significantly enhanced the apoptogenic potency of Cyt c(77-101) to a concentration readily achievable in vivo. Moreover, this construct, Nup153-Cyt c, facilitates the dramatic redistribution of nuclear pore complex proteins and thus propounds the nuclear pore complex as a novel target for the therapeutic induction of apoptosis.
Authors
I am an author on this paper
Click your name to claim this paper and add it to your profile.
Reviews
Recommended
No Data Available