The Polymorphic Nature of Membrane-Active Peptides from Biophysical and Structural Investigations

Author(s): Burkhard Bechinger, Christopher Aisenbrey

Journal Name: Current Protein & Peptide Science

Volume 13 , Issue 7 , 2012


Become EABM
Become Reviewer
Call for Editor

Abstract:

Membrane-active peptides exhibit a wide variety of biological functions including pore formation, signaling and antimicrobial activities. They are also capable of transporting large cargo such as proteins or nucleic acids across cell membranes. This review summarizes biophysical and structural investigations on hydrophobic, amphipathic and heavily charged peptides that reveal a very dynamic view on their membrane interactions. Individual peptides are able to adopt a variety of different conformations and topology and at the same time exhibit multimodal functionalities. Examples discussed in this paper include peptaibols, magainins, cell penetrating peptides and designed histidine-rich sequences with potent antimicrobial and nucleic acid transfection activities.

Keywords: Alamethicin, cecropin, hydrophobic mismatch, membrane topology, solid-state NMR, supported bilayers.

Rights & PermissionsPrintExport Cite as

Article Details

VOLUME: 13
ISSUE: 7
Year: 2012
Published on: 25 November, 2012
Page: [602 - 610]
Pages: 9
DOI: 10.2174/138920312804142093
Price: $65

Article Metrics

PDF: 12