Cookies on this website

We use cookies to ensure that we give you the best experience on our website. If you click 'Accept all cookies' we'll assume that you are happy to receive all cookies and you won't see this message again. If you click 'Reject all non-essential cookies' only necessary cookies providing core functionality such as security, network management, and accessibility will be enabled. Click 'Find out more' for information on how to change your cookie settings.

We designed and synthesized an 18 residue peptide (MS18) similar to the channel forming fungal antibiotic alamethicin. MS18 formed ion channels in lipid bilayers exhibiting a low discrete conductance level of 55 pS and brief openings to many other conductance levels. Channel formation was markedly dopondonl on transbilayer voltage with macroscopic conductance increasing exponentially beyond an activation voltage. The activation voltage was higher for lower concentrations of peptide. The relationship between conductance, voltage and peptide concentration was used to calculate the mean number of peptide monomers forming the MS18 channel. This gave an estimate of 4 MS18 monomers per channel. Molecular modeling of MS18 revealed a predominantly α-helical structure.


Journal article


Cellular and Molecular Biology Letters

Publication Date





325 - 336