The Library
Helical membrane peptides to modulate cell function
Tools
Beevers, Andrew J. and Dixon, Ann M. (2010) Helical membrane peptides to modulate cell function. Chemical Society Reviews, Vol.39 (No.6). pp. 2146-2157. doi:10.1039/b912944h
Research output not available from this repository.
Request-a-Copy directly from author or use local Library Get it For Me service.
Official URL: http://dx.doi.org/10.1039/b912944h
Abstract
In recent years there has been an abundance of research into the potential of helical peptides to influence cell function. These peptides have been used to achieve a variety of different outcomes from cell repair to cell death, depending upon the peptide sequence and the nature of its interactions with cell membranes and membrane proteins. In this critical review, we summarise several mechanisms by which helical peptides, acting as either transporters, inhibitors, agonists or antibiotics, can have significant effects on cell membranes and can radically affect the internal mechanisms of the cell. The various approaches to peptide design are discussed, including the role of naturally-occurring proteins in the design of these helical peptides and current breakthroughs in the use of non-natural (and therefore more stable) peptide scaffolds. Most importantly, the current successful applications of these peptides, and their potential uses in the field of medicine, are reviewed.
Item Type: | Journal Item | ||||
---|---|---|---|---|---|
Subjects: | Q Science > QD Chemistry Q Science > QP Physiology |
||||
Divisions: | Faculty of Science, Engineering and Medicine > Science > Chemistry | ||||
Library of Congress Subject Headings (LCSH): | Peptides, Cell physiology, Cellular signal transduction, Cell membranes | ||||
Journal or Publication Title: | Chemical Society Reviews | ||||
Publisher: | Royal Society of Chemistry | ||||
ISSN: | 0306-0012 | ||||
Official Date: | June 2010 | ||||
Dates: |
|
||||
Volume: | Vol.39 | ||||
Number: | No.6 | ||||
Number of Pages: | 12 | ||||
Page Range: | pp. 2146-2157 | ||||
DOI: | 10.1039/b912944h | ||||
Status: | Peer Reviewed | ||||
Publication Status: | Published | ||||
Access rights to Published version: | Restricted or Subscription Access |
Data sourced from Thomson Reuters' Web of Knowledge
Request changes or add full text files to a record
Repository staff actions (login required)
View Item |