Journal
JOURNAL OF BIOLOGICAL PHYSICS
Volume 33, Issue 5-6, Pages 345-356Publisher
SPRINGER
DOI: 10.1007/s10867-008-9074-3
Keywords
Cell penetrating peptides; Drug delivery; Arginine-rich peptide; Cellular uptake mechanism; Intracellular protein delivery; Membrane translocation; Antimicrobial peptides; Peptide uptake
Categories
Funding
- National Science Foundation [DMR-0117792]
- Rensselaer Polytechnic Institute
Ask authors/readers for more resources
Cell penetrating peptides consist of short sequences of amino acids containing a large net positive charge that are able to penetrate almost any cell, carrying with them relatively large cargoes such as proteins, oligonucleotides, and drugs. During the 10 years since their discovery, the question of how they manage to translocate across the membrane has remained unanswered. The main discussion has been centered on whether they follow an energy-independent or an energy-dependent pathway. Recently, we have discovered the possibility of an energy-independent pathway that challenges fundamental concepts associated with protein-membrane interactions (Herce and Garcia, PNAS, 104: 20805 (2007) [1]). It involves the translocation of charged residues across the hydrophobic core of the membrane and the passive diffusion of these highly charged peptides across the membrane through the formation of aqueous toroidal pores. The aim of this review is to discuss the details of the mechanism and interpret some experimental results consistent with this view.
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