Antimicrobial peptides at work: Interaction of myxinidin and its mutant WMR with lipid bilayers mimicking the P. aeruginosa and E. coli membranes

L. Lombardi; M.I. Stellato; R. Oliva; A. Falanga; M. Galdiero; L. Petraccone; G. D'Errico; A. De Santis; S. Galdiero; P. Del Vecchio

doi:10.1038/srep44425

Antimicrobial peptides at work: Interaction of myxinidin and its mutant WMR with lipid bilayers mimicking the P. aeruginosa and E. coli membranes

L. Lombardi, M.I. Stellato, R. Oliva, A. Falanga, M. Galdiero, L. Petraccone, G. D'Errico, A. De Santis, S. Galdiero, P. Del Vecchio

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Abstract

Antimicrobial peptides are promising candidates as future therapeutics in order to face the problem
of antibiotic resistance caused by pathogenic bacteria. Myxinidin is a peptide derived from the hagfish
mucus displaying activity against a broad range of bacteria. We have focused our studies on the
physico-chemical characterization of the interaction of myxinidin and its mutant WMR, which contains
a tryptophan residue at the N-terminus and four additional positive charges, with two model biological
membranes (DOPE/DOPG 80/20 and DOPE/DOPG/CL 65/23/12), mimicking respectively Escherichia coli
and Pseudomonas aeruginosa membrane bilayers. All our results have coherently shown that, although
both myxinidin and WMR interact with the two membranes, their effect on membrane microstructure
and stability are different. We further have shown that the presence of cardiolipin plays a key role in the
WMR-membrane interaction. Particularly, WMR drastically perturbs the DOPE/DOPG/CL membrane
stability inducing a segregation of anionic lipids. On the contrary, myxinidin is not able to significantly
perturb the DOPE/DOPG/CL bilayer whereas interacts better with the DOPE/DOPG bilayer causing a
significant perturbing effect of the lipid acyl chains. These findings are fully consistent with the reported
greater antimicrobial activity of WMR against P. aeruginosa compared with myxinidin.

Original language	English
Article number	4425
Number of pages	15
Journal	Scientific Reports
Volume	7
Issue number	44425
DOIs	https://doi.org/10.1038/srep44425
Publication status	Published - 15 Mar 2017
Externally published	Yes

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10.1038/srep44425Licence: CC BY

Antimicrobial peptides at work: interaction of myxinidin and its mutant WMR with lipid bilayers mimicking the P. aeruginosa and E. coli membranes
© 2017 The Authors. This is an open access article published under a Creative Commons Attribution License (https://creativecommons.org/licenses/by/4.0/), which permits unrestricted use, distribution and reproduction in any medium, provided the author and source are cited.
Final published version, 2.21 MBLicence: CC BY

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Lombardi, L., Stellato, M. I., Oliva, R., Falanga, A., Galdiero, M., Petraccone, L., D'Errico, G., De Santis, A., Galdiero, S., & Del Vecchio, P. (2017). Antimicrobial peptides at work: Interaction of myxinidin and its mutant WMR with lipid bilayers mimicking the P. aeruginosa and E. coli membranes. Scientific Reports, 7(44425), Article 4425 . https://doi.org/10.1038/srep44425

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title = "Antimicrobial peptides at work: Interaction of myxinidin and its mutant WMR with lipid bilayers mimicking the P. aeruginosa and E. coli membranes",

abstract = "Antimicrobial peptides are promising candidates as future therapeutics in order to face the problemof antibiotic resistance caused by pathogenic bacteria. Myxinidin is a peptide derived from the hagfishmucus displaying activity against a broad range of bacteria. We have focused our studies on thephysico-chemical characterization of the interaction of myxinidin and its mutant WMR, which containsa tryptophan residue at the N-terminus and four additional positive charges, with two model biologicalmembranes (DOPE/DOPG 80/20 and DOPE/DOPG/CL 65/23/12), mimicking respectively Escherichia coliand Pseudomonas aeruginosa membrane bilayers. All our results have coherently shown that, althoughboth myxinidin and WMR interact with the two membranes, their effect on membrane microstructureand stability are different. We further have shown that the presence of cardiolipin plays a key role in theWMR-membrane interaction. Particularly, WMR drastically perturbs the DOPE/DOPG/CL membranestability inducing a segregation of anionic lipids. On the contrary, myxinidin is not able to significantlyperturb the DOPE/DOPG/CL bilayer whereas interacts better with the DOPE/DOPG bilayer causing asignificant perturbing effect of the lipid acyl chains. These findings are fully consistent with the reportedgreater antimicrobial activity of WMR against P. aeruginosa compared with myxinidin.",

author = "L. Lombardi and M.I. Stellato and R. Oliva and A. Falanga and M. Galdiero and L. Petraccone and G. D'Errico and {De Santis}, A. and S. Galdiero and {Del Vecchio}, P.",

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AU - Lombardi, L.

AU - Stellato, M.I.

AU - Oliva, R.

AU - Falanga, A.

AU - Galdiero, M.

AU - Petraccone, L.

AU - D'Errico, G.

AU - De Santis, A.

AU - Galdiero, S.

AU - Del Vecchio, P.

PY - 2017/3/15

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N2 - Antimicrobial peptides are promising candidates as future therapeutics in order to face the problemof antibiotic resistance caused by pathogenic bacteria. Myxinidin is a peptide derived from the hagfishmucus displaying activity against a broad range of bacteria. We have focused our studies on thephysico-chemical characterization of the interaction of myxinidin and its mutant WMR, which containsa tryptophan residue at the N-terminus and four additional positive charges, with two model biologicalmembranes (DOPE/DOPG 80/20 and DOPE/DOPG/CL 65/23/12), mimicking respectively Escherichia coliand Pseudomonas aeruginosa membrane bilayers. All our results have coherently shown that, althoughboth myxinidin and WMR interact with the two membranes, their effect on membrane microstructureand stability are different. We further have shown that the presence of cardiolipin plays a key role in theWMR-membrane interaction. Particularly, WMR drastically perturbs the DOPE/DOPG/CL membranestability inducing a segregation of anionic lipids. On the contrary, myxinidin is not able to significantlyperturb the DOPE/DOPG/CL bilayer whereas interacts better with the DOPE/DOPG bilayer causing asignificant perturbing effect of the lipid acyl chains. These findings are fully consistent with the reportedgreater antimicrobial activity of WMR against P. aeruginosa compared with myxinidin.

AB - Antimicrobial peptides are promising candidates as future therapeutics in order to face the problemof antibiotic resistance caused by pathogenic bacteria. Myxinidin is a peptide derived from the hagfishmucus displaying activity against a broad range of bacteria. We have focused our studies on thephysico-chemical characterization of the interaction of myxinidin and its mutant WMR, which containsa tryptophan residue at the N-terminus and four additional positive charges, with two model biologicalmembranes (DOPE/DOPG 80/20 and DOPE/DOPG/CL 65/23/12), mimicking respectively Escherichia coliand Pseudomonas aeruginosa membrane bilayers. All our results have coherently shown that, althoughboth myxinidin and WMR interact with the two membranes, their effect on membrane microstructureand stability are different. We further have shown that the presence of cardiolipin plays a key role in theWMR-membrane interaction. Particularly, WMR drastically perturbs the DOPE/DOPG/CL membranestability inducing a segregation of anionic lipids. On the contrary, myxinidin is not able to significantlyperturb the DOPE/DOPG/CL bilayer whereas interacts better with the DOPE/DOPG bilayer causing asignificant perturbing effect of the lipid acyl chains. These findings are fully consistent with the reportedgreater antimicrobial activity of WMR against P. aeruginosa compared with myxinidin.

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Antimicrobial peptides at work: Interaction of myxinidin and its mutant WMR with lipid bilayers mimicking the P. aeruginosa and E. coli membranes

Abstract

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