Journal
CURRENT PROTEIN & PEPTIDE SCIENCE
Volume 13, Issue 7, Pages 602-610Publisher
BENTHAM SCIENCE PUBL LTD
DOI: 10.2174/138920312804142093
Keywords
Alamethicin; cecropin; hydrophobic mismatch; membrane topology; solid-state NMR; supported bilayers
Categories
Funding
- Agence Nationale de la Recherche
- Region Alsace
- CNRS
- University of Strasbourg
- Vaincre la Mucoviscidose (French Cystic Fibrosis association)
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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.
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