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Phospholipid dependent mechanism of smp24, an α-helical antimicrobial peptide from scorpion venom

Harrison, Patrick L.; Heath, George R.; Johnson, Benjamin R.G.; Abdel-Rahman, Mohamed A.; Strong, Peter N.; Evans, Stephen D.; Miller, Keith


Patrick L. Harrison

George R. Heath

Benjamin R.G. Johnson

Mohamed A. Abdel-Rahman

Peter N. Strong

Stephen D. Evans

Keith Miller


Determining the mechanism of action of antimicrobial peptides (AMPs) is critical if they are to be developed into the clinical setting. In recent years high resolution techniques such as atomic force microscopy (AFM) have increasingly been utilised to determine AMP mechanism of action on planar lipid bilayers and live bacteria. Here we present the biophysical characterisation of a prototypical AMP from the venom of the North African scorpion Scorpio maurus palmatus termed Smp24. Smp24 is an amphipathic helical peptide containing 24 residues with a charge of + 3 and exhibits both antimicrobial and cytotoxic activity and we aim to elucidate the mechanism of action of this peptide on both membrane systems.

Using AFM, quartz crystal microbalance-dissipation (QCM-D) and liposomal leakage assays the effect of Smp24 on prototypical synthetic prokaryotic (DOPG:DOPC) and eukaryotic (DOPE:DOPC) membranes has been determined. Our data points to a toroidal pore mechanism against the prokaryotic like membrane whilst the formation of hexagonal phase non-lamellar phase structures is seen in eukaryotic like membrane. Also, phase segregation is observed against the eukaryotic membrane and this study provides direct evidence of the same peptide having multiple mechanisms of action depending on the membrane lipid composition.


Harrison, P. L., Heath, G. R., Johnson, B. R., Abdel-Rahman, M. A., Strong, P. N., Evans, S. D., & Miller, K. (2016). Phospholipid dependent mechanism of smp24, an α-helical antimicrobial peptide from scorpion venom. BBA - Biomembranes, 1858(11), 2737-2744.

Journal Article Type Article
Acceptance Date Jul 27, 2016
Online Publication Date Jul 30, 2016
Publication Date 2016-11
Deposit Date May 7, 2019
Publicly Available Date May 8, 2019
Journal Biochimica et Biophysica Acta - Biomembranes
Print ISSN 0005-2736
Electronic ISSN 1879-2642
Publisher Elsevier
Peer Reviewed Peer Reviewed
Volume 1858
Issue 11
Pages 2737-2744
Keywords Antimicrobial peptides; Membrane damage; Atomic force microscopy; Quartz crystal microbalance-dissipation
Public URL
Publisher URL
Additional Information This article is maintained by: Elsevier; Article Title: Phospholipid dependent mechanism of smp24, an α-helical antimicrobial peptide from scorpion venom; Journal Title: Biochimica et Biophysica Acta (BBA) - Biomembranes; CrossRef DOI link to publisher maintained version:; Content Type: article; Copyright: © 2016 The Authors. Published by Elsevier B.V.


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