C-end rule peptides mediate neuropilin-1-dependent cell, vascular, and tissue penetration
University of California, Santa Barbara · Sanford Burnham Prebys Medical Discovery Institute · +1 more institution
Abstract
Screening of phage libraries expressing random peptides for binding to prostate cancer cells primarily yielded peptides that had a C-terminal arginine (or rarely lysine) residue, usually in a consensus context R/KXXR/K. Phage expressing these sequences and synthetic nanoparticles coated with them bound to and were internalized into cells. The C-terminal arginine (or lysine) was essential to the activity; adding another amino acid, or even blocking the free carboxyl group of this arginine residue by amidation, eliminated the binding and internalizing activity. An internal R/KXXR/K can be exposed and switched on by a cleavage by a protease. The strict requirement for C-terminal exposure of the motif prompted us…
Citation impact
- FWCI
- 8.21
- Percentile
- 100%
- References
- 37
Authors
4- TTTambet TeesaluCorresponding
University of California, Santa Barbara, Sanford Burnham Prebys Medical Discovery Institute
- KNKazuki N. Sugahara
University of California, Santa Barbara, Sanford Burnham Prebys Medical Discovery Institute
- VRVenkata Ramana Kotamraju
University of California, Santa Barbara, Sanford Burnham Prebys Medical Discovery Institute
- ERErkki Ruoslahti
University of California, Santa Barbara, Sanford Burnham Prebys Medical Discovery Institute, Cancer Research Center
Topics & keywords
- Arginine
- Peptide
- Internalization
- Neuropilin 1
- Phage display
- Biochemistry
- Protease
- Lysine
- Good health and well-being