Biosynthesis of alamethicin

Lipid-alamethicin interactions influence alamethicin orientation.

Whereas the barrel-stave configuration is accepted by most investigators as a good description of the conducting state of alamethicin, there are conflicting interpretations on its nonconducting state; in the absence of an applied field, some found alamethicin molecules on the membrane surface, but others found them incorporated in the hydrophobic core of the membrane. This problem is resolved b...

Recent Results of Alamethicin Research

Interaction of alamethicin pores in DMPC bilayers.

We have investigated the x-ray scattering signal of highly aligned multilayers of the zwitterionic lipid 1,2-dimyristoyl-sn-glycero-3-phosphatidylcholine containing pores formed by the antimicrobial peptide alamethicin as a function of the peptide/lipid ratio. We are able to obtain information on the structure factor of the pore fluid, which then yields the interaction potential between pores i...

The nature and function of alamethicin.

The tubulin-rich fraction was also shown to contain a protein subunit, of mol.wt. 46000f 1500, identified as actin by co-electrophoresis with skeletal-muscle actin. Although actin can be removed from brain tubulin preparations by repeated cycles of depolymerization/polymerization, its total removal from the platelet tubulin-rich fraction is most difEcult. In addition to tubulin and actin, three...

Alamethicin-mediated fusion of lecithin vesicles.

It was recently shown that alamethicin greatly facilitates the fusion of small, sonicated, lecithin bilayer vesicles. In the present work the details of this fusion process have been followed by monitoring the inner and outer choline methyl signals separately by proton magnetic resonance spectroscopy. It is shown that during the alamethicine-induced fusion some of the antibiotic molecules becom...