Structure and Functions of Channel-Forming Peptides: Magainins, Cecropins, Melittin and Alamethicin

Structure and Functions of Channel-Forming Peptides: Magainins, Cecropins, Melittin and Alamethicin J. Membrane Biol. 156, 197–211 (1997) The Journal of Membrane Biology © Springer-Verlag New York Inc. 1997 Topical Review Structure and Functions of Channel-Forming Peptides: Magainins, Cecropins, Melittin and Alamethicin B. Bechinger Max-Planck-Institut fu ¨ r Biochemie, Am Klopferspitz 18a, 82152 Martinsried, Germany Received: 25 November 1996/Revised: 6 December 1996 Introduction interest for pharmacological applications are those which manifest immunological or tumoricidal activity, but un- der the same conditions, do not show hemolytic or cy- Membrane-active peptides exhibit many interesting bio- totoxic activity against healthy vertebrate cells [123]. logical and pharmacological activities. These peptides Membrane-active peptides also exhibit channel-like con- can be synthesized and purified by chemical or bio- ductivities across planar lipid bilayer systems as well as chemical means in sufficient quantities to allow for their bilayer disruption. These bilayer openings deprive the study by biophysical techniques. Whereas the character- affected organisms of their transmembrane electrochemi- istics and biological activities of some of these peptides cal gradients, result in increased water flow concomitant are highly interesting in themselves, they also provide with cell swelling, osmolysis and cell death. A detailed model systems for large membrane proteins. The study understanding of the mechanisms of channel-formation of these peptides therefore http://www.deepdyve.com/assets/images/DeepDyve-Logo-lg.png The Journal of Membrane Biology Springer Journals

Structure and Functions of Channel-Forming Peptides: Magainins, Cecropins, Melittin and Alamethicin

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Publisher
Springer-Verlag
Copyright
Copyright © Inc. by 1997 Springer-Verlag New York
Subject
Life Sciences; Biochemistry, general; Human Physiology
ISSN
0022-2631
eISSN
1432-1424
D.O.I.
10.1007/s002329900201
Publisher site
See Article on Publisher Site

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