Alamethicin is an antibiotic peptide.
Plenty of peptide antibiotics have been identified in the past half-century, falling into two classes, non-ribosomally synthesized peptides, such as polymyxins, gramicidins, bacitracins, glycopeptides, and ribosomally synthesized (natural) peptides. The former are usually modified and produced by bacteria, while the latter are produced by all species as a major component of the host defense molecules.
In vitro: Alamethicin was identified as an antibiotic peptide belonging to membrane active peptides of fungal origin with an unusual amphiphilic amino acid, 2-aminoisobutyric acid, which can induce helical peptide structures strongly, leading to the formation of voltage-gated ion channels in the cell membrane bilayers. Alamethicin is also widely used as agent to induce various defense responses and physiological in eukaryotic cells [1]. In addition, alamethicin was quite often used to evaluate voltage gating, ion channel assembly, as well as peptide-membrane interactions [2, 3].
In vivo: Up to now, alamethicin is only for in-vitro usage and there is no animal in-vivo study reported.
Clinical trial: So far, no clinical study has been conducted.
References:
[1] Maischak, H. ,Zimmermann, M.R.,Felle, H.H., et al. Alamethicin-induced electrical long distance signaling in plants. Plant Signal.Behav. 5(8), 988-990 (2010).
[2] Jones, L. R.,Maddock, S.W. and Besch, H.R., Jr. Unmasking effect of alamethicin on the (Na+,K+)-ATPase, β-adrenergic receptor-coupled adenylate cyclase, and cAMP-dependent protein kinase activities of cardiac sarcolemmal vesicles. The Journal of Biological Chemisty 255(20), 9971-9980 (1980).
[3] Pan, J. ,Tristram-Nagle, S. and Nagle, J.F. Alamethicin aggregation in lipid membranes. Journal of Membrane Biology 231(1), 1-36 (2009).