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

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 lipi...

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Published inBiochimica et biophysica acta Vol. 1858; no. 11; pp. 2737 - 2744
Main Authors Harrison, Patrick L., Heath, George R., Johnson, Benjamin R.G., Abdel-Rahman, Mohamed A., Strong, Peter N., Evans, Stephen D., Miller, Keith
Format Journal Article
LanguageEnglish
Published Netherlands Elsevier B.V 01.11.2016
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Abstract 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. [Display omitted] •Determination of antimicrobial peptide mechanism of action using AFM & QCM-D•Toroidal pore mechanism seen in prokaryotic model membranes following exposure to smp24•Non-lamellar phase and lipid segregation seen with eukaryotic model membranes following exposure to smp24
AbstractList 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.
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. [Display omitted] •Determination of antimicrobial peptide mechanism of action using AFM & QCM-D•Toroidal pore mechanism seen in prokaryotic model membranes following exposure to smp24•Non-lamellar phase and lipid segregation seen with eukaryotic model membranes following exposure to smp24
Author Evans, Stephen D.
Strong, Peter N.
Miller, Keith
Abdel-Rahman, Mohamed A.
Johnson, Benjamin R.G.
Harrison, Patrick L.
Heath, George R.
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Issue 11
Keywords Atomic force microscopy
Quartz crystal microbalance-dissipation
Membrane damage
Antimicrobial peptides
Language English
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Snippet 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...
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SubjectTerms Animals
Antimicrobial Cationic Peptides - chemical synthesis
Antimicrobial Cationic Peptides - pharmacology
Antimicrobial peptides
Atomic force microscopy
Lipid Bilayers - chemistry
Liposomes - chemistry
Membrane damage
Molecular Mimicry
Phosphatidylcholines - chemistry
Phosphatidylethanolamines - chemistry
Phosphatidylglycerols - chemistry
Protein Conformation, alpha-Helical
Quartz crystal microbalance-dissipation
Scorpion Venoms - chemical synthesis
Scorpion Venoms - pharmacology
Scorpions - chemistry
Static Electricity
Title Phospholipid dependent mechanism of smp24, an α-helical antimicrobial peptide from scorpion venom
URI https://dx.doi.org/10.1016/j.bbamem.2016.07.018
https://www.ncbi.nlm.nih.gov/pubmed/27480803
https://search.proquest.com/docview/1826742833
Volume 1858
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