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The peptide alamethicin forms channels with a variety of conductance states. Selective stabilization of a particular state should simplify the task of understanding conductance in terms of channel structure. We synthesized two different covalent dimers of alamethicin in which peptides were linked at their C-terminal ends by flexible tethers. Both dimeric peptides formed channels with conductances that matched those of alamethicin channels. Particular conductance states were selectively stabilized, however, with lifetimes up to 170-fold longer than the same states observed with monomers. In addition, tethering appeared to limit the size of the structures formed so that, even at higher peptide concentrations, a single predominant conductance state was obtained. We suggest this state corresponds to a channel made from six alamethicin molecules (three dimers).

Original publication

DOI

10.1021/bi9529216

Type

Journal article

Journal

Biochemistry

Publication Date

21/05/1996

Volume

35

Pages

6225 - 6232

Keywords

Alamethicin, Amino Acid Sequence, Drug Stability, Electric Conductivity, In Vitro Techniques, Ion Channels, Models, Molecular, Molecular Sequence Data, Molecular Structure, Protein Conformation, Protein Engineering