One pathogen two stones: are Australian tree frog antimicrobial peptides synergistic against human pathogens?
Identifieur interne : 000688 ( Main/Exploration ); précédent : 000687; suivant : 000689One pathogen two stones: are Australian tree frog antimicrobial peptides synergistic against human pathogens?
Auteurs : Marc-Antoine Sani [Australie] ; Siobhan Carne [Australie] ; Sarah A. Overall [Australie] ; Alexandre Poulhazan [Australie] ; Frances Separovic [Australie]Source :
- European biophysics journal : EBJ [ 1432-1017 ] ; 2017.
Abstract
Antimicrobial peptides (AMPs) may act by targeting the lipid membranes and disrupting the bilayer structure. In this study, three AMPs from the skin of Australian tree frogs, aurein 1.2, maculatin 1.1 and caerin 1.1, were investigated against Gram-negative Escherichia coli, Gram-positive Staphylococcus aureus, and vesicles that mimic their lipid compositions. Furthermore, equimolar mixtures of the peptides were tested to identify any synergistic interactions in antimicrobial activity. Minimum inhibition concentration and minimum bactericidal concentration assays showed significant activity against S. aureus but not against E. coli. Aurein was the least active while maculatin was the most active peptide and some synergistic effects were observed against S. aureus. Circular dichroism experiments showed that, in the presence of phospholipid vesicles, the peptides transitioned from an unstructured to a predominantly helical conformation (>50%), with greater helicity for POPG/TOCL compared to POPE/POPG vesicles. The helical content, however, was less in the presence of live E. coli and S. aureus, 25 and 5%, respectively. Equimolar concentrations of the peptides did not appear to form greater supramolecular structures. Dye release assays showed that aurein required greater concentration than caerin and maculatin to disrupt the lipid bilayers, and mixtures of the peptides did not cooperate to enhance their lytic activity. Overall, aurein, maculatin, and caerin showed moderate synergy in antimicrobial activity against S. aureus without becoming more structured or enhancement of their membrane-disrupting activity in phospholipid vesicles.
DOI: 10.1007/s00249-017-1215-9
PubMed: 28478484
Affiliations:
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Overall</name><affiliation wicri:level="4"><nlm:affiliation>School of Chemistry, Bio21 Institute, University of Melbourne, Melbourne, VIC, 3010, Australia.</nlm:affiliation><country xml:lang="fr">Australie</country><wicri:regionArea>School of Chemistry, Bio21 Institute, University of Melbourne, Melbourne, VIC, 3010</wicri:regionArea><orgName type="university">Université de Melbourne</orgName><placeName><settlement type="city">Melbourne</settlement><region type="état">Victoria (État)</region></placeName></affiliation></author><author><name sortKey="Poulhazan, Alexandre" sort="Poulhazan, Alexandre" uniqKey="Poulhazan A" first="Alexandre" last="Poulhazan">Alexandre Poulhazan</name><affiliation wicri:level="4"><nlm:affiliation>School of Chemistry, Bio21 Institute, University of Melbourne, Melbourne, VIC, 3010, Australia.</nlm:affiliation><country xml:lang="fr">Australie</country><wicri:regionArea>School of Chemistry, Bio21 Institute, University of Melbourne, Melbourne, VIC, 3010</wicri:regionArea><orgName type="university">Université de Melbourne</orgName><placeName><settlement type="city">Melbourne</settlement><region type="état">Victoria (État)</region></placeName></affiliation></author><author><name sortKey="Separovic, Frances" sort="Separovic, Frances" uniqKey="Separovic F" first="Frances" last="Separovic">Frances Separovic</name><affiliation wicri:level="4"><nlm:affiliation>School of Chemistry, Bio21 Institute, University of Melbourne, Melbourne, VIC, 3010, Australia. fs@unimelb.edu.au.</nlm:affiliation><country xml:lang="fr">Australie</country><wicri:regionArea>School of Chemistry, Bio21 Institute, University of Melbourne, Melbourne, VIC, 3010</wicri:regionArea><orgName type="university">Université de Melbourne</orgName><placeName><settlement type="city">Melbourne</settlement><region type="état">Victoria (État)</region></placeName></affiliation></author></analytic><series><title level="j">European biophysics journal : EBJ</title><idno type="eISSN">1432-1017</idno><imprint><date when="2017" type="published">2017</date></imprint></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">Antimicrobial peptides (AMPs) may act by targeting the lipid membranes and disrupting the bilayer structure. In this study, three AMPs from the skin of Australian tree frogs, aurein 1.2, maculatin 1.1 and caerin 1.1, were investigated against Gram-negative Escherichia coli, Gram-positive Staphylococcus aureus, and vesicles that mimic their lipid compositions. Furthermore, equimolar mixtures of the peptides were tested to identify any synergistic interactions in antimicrobial activity. Minimum inhibition concentration and minimum bactericidal concentration assays showed significant activity against S. aureus but not against E. coli. Aurein was the least active while maculatin was the most active peptide and some synergistic effects were observed against S. aureus. Circular dichroism experiments showed that, in the presence of phospholipid vesicles, the peptides transitioned from an unstructured to a predominantly helical conformation (>50%), with greater helicity for POPG/TOCL compared to POPE/POPG vesicles. The helical content, however, was less in the presence of live E. coli and S. aureus, 25 and 5%, respectively. Equimolar concentrations of the peptides did not appear to form greater supramolecular structures. Dye release assays showed that aurein required greater concentration than caerin and maculatin to disrupt the lipid bilayers, and mixtures of the peptides did not cooperate to enhance their lytic activity. Overall, aurein, maculatin, and caerin showed moderate synergy in antimicrobial activity against S. aureus without becoming more structured or enhancement of their membrane-disrupting activity in phospholipid vesicles.</div></front></TEI><affiliations><list><country><li>Australie</li></country><region><li>Victoria (État)</li></region><settlement><li>Melbourne</li></settlement><orgName><li>Université de Melbourne</li></orgName></list><tree><country name="Australie"><region name="Victoria (État)"><name sortKey="Sani, Marc Antoine" sort="Sani, Marc Antoine" uniqKey="Sani M" first="Marc-Antoine" last="Sani">Marc-Antoine Sani</name></region><name sortKey="Carne, Siobhan" sort="Carne, Siobhan" uniqKey="Carne S" first="Siobhan" last="Carne">Siobhan Carne</name><name sortKey="Overall, Sarah A" sort="Overall, Sarah A" uniqKey="Overall S" first="Sarah A" last="Overall">Sarah A. Overall</name><name sortKey="Poulhazan, Alexandre" sort="Poulhazan, Alexandre" uniqKey="Poulhazan A" first="Alexandre" last="Poulhazan">Alexandre Poulhazan</name><name sortKey="Separovic, Frances" sort="Separovic, Frances" uniqKey="Separovic F" first="Frances" last="Separovic">Frances Separovic</name></country></tree></affiliations></record>Pour manipuler ce document sous Unix (Dilib)
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