Maculatin 1.1 Disrupts Staphylococcus aureus Lipid Membranes via a Pore Mechanism

Sani, Marc‐Antoine; Whitwell, Thomas; Gehman, John D.; Robins-Browne, Roy M.; Pantarat, Namfon; Attard, Troy J.; Reynolds, Eric C.; O'Brien-Simpson, Neil M; Separovic, Frances

doi:10.1128/aac.00195-13

Cited by 41 publications

(51 citation statements)

References 29 publications

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“…7A). Acquisition of an ␣-helical conformation when in a membrane environment is consistent with previous studies (13,14). Interestingly, the CD spectrum of Mac1 in the presence of PC/SM/Chol was similar to the one obtained in buffer, indicating that the majority of the peptide molecules are in a random conformation, in agreement with Mac1 binding weakly to this particular membrane composition.…”

Section: Mac1 Has Higher Helical Content In Charged Lipidsupporting

confidence: 79%

“…Mac1 and melittin have been used in many experiments without showing any solubility or secondary structure perturbations in buffer with up to 150 mM NaCl (14,15,25). Therefore, it may be that bacteria are able to withstand harsh membrane damage in high salt (LB) compared with low salt growth medium (MHB).…”

Section: Mac1 Has Antimicrobial Activity Against S Aureus and E Colmentioning

confidence: 99%

“…Previous studies have shown that Mac1 adopts an ␣-helical secondary structure in contact with lipid membranes (13). The helical peptide is amphipathic and can insert into lipid bilayers, eventually forming pores (14).…”

mentioning

confidence: 99%

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Bacteria May Cope Differently from Similar Membrane Damage Caused by the Australian Tree Frog Antimicrobial Peptide Maculatin 1.1

Sani

Henriques

Weber

et al. 2015

Journal of Biological Chemistry

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Background: Mac1 specificity and bactericidal concentrations may be due to a distinctive membrane disrupting mechanism. Results: S. aureus growth is inhibited at 16-fold lower Mac1 concentration than E. coli, but both lipid membranes are compromised at similar concentrations. Conclusion: Bacteria may cope differently with membrane damage. Significance: Antimicrobial peptide mode of action needs to be better understood to develop new drug candidate.

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Section: Mac1 Has Higher Helical Content In Charged Lipidsupporting

confidence: 79%

Section: Mac1 Has Antimicrobial Activity Against S Aureus and E Colmentioning

confidence: 99%

See 1 more Smart Citation

Bacteria May Cope Differently from Similar Membrane Damage Caused by the Australian Tree Frog Antimicrobial Peptide Maculatin 1.1

Sani

Henriques

Weber

et al. 2015

Journal of Biological Chemistry

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“…The MIC was determined by plotting maximal growth versus peptide concentration, according to the Lambert and Pearson analysis method, while MBC was confirmed via colony-forming unit (CFU) measuring assay (Lambert and Pearson, 2000;Sani et al, 2013). The MIC and MBC values for the monomer and dimer were similar to that induced by the tetramer (Table 1).…”

Section: Synthesis Of Chex-arg20 Multimer Analogsmentioning

confidence: 99%

Multimerization of a Proline-Rich Antimicrobial Peptide, Chex-Arg20, Alters Its Mechanism of Interaction with the Escherichia coli Membrane

O'Brien-Simpson

Tailhades

et al. 2015

Chemistry & Biology

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A3-APO, a de novo designed branched dimeric proline-rich antimicrobial peptide (PrAMP), is highly effective against a variety of in vivo bacterial infections. We undertook a selective examination of the mechanism for the Gram-negative Escherichia coli bacterial membrane interaction of the monomer (Chex-Arg20), dimer (A3-APO), and tetramer (A3-APO disulfide-linked dimer). All three synthetic peptides were effective at killing E. coli. However, the tetramer was 30-fold more membrane disruptive than the dimer while the monomer showed no membrane activity. Using flow cytometry and high-resolution fluorescent microscopy, it was observed that dimerization and tetramerization of the Chex-Arg20 monomer led to an alteration in the mechanism of action from non-lytic/membrane hyperpolarization to membrane disruption/depolarization. Our findings show that the membrane interaction and permeability of Chex-Arg20 was altered by multimerization.

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“…Although the mechanism of AMP action is unknown and pore formation in cell membranes may be responsible for lytic ability, it is well established that AMP interact directly with the cell membrane surface and are able to enter the lipid bilayer, resulting in cell membrane disruption and leakage of cytoplasmic components which leads to killing of microbes (Lee et al 2010;Izadpanah and Gallo 2005;Lorenzon et al 2012;Sani et al 2013). AMP have attracted much attention as an alternative to antibiotics because of their effect against bacterial infections and drug resistant bacteria (Juba et al 2013;AnayaLopez et al 2013).…”

Section: Introductionmentioning

confidence: 96%

Melittin peptides exhibit different activity on different cells and model membranes

et al. 2014

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was increased. The native peptide and the MLT-P14C monomer were mainly unstructured in buffer while the dimer adopted a helical conformation. In the presence of neutral and negatively charged vesicles, the helical content of the three peptides was significantly increased. The lytic activity, therefore, is not correlated to the secondary structure of the peptides and, more particularly, on the propensity to adopt helical conformation.

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Maculatin 1.1 Disrupts Staphylococcus aureus Lipid Membranes via a Pore Mechanism

Cited by 41 publications

References 29 publications

Bacteria May Cope Differently from Similar Membrane Damage Caused by the Australian Tree Frog Antimicrobial Peptide Maculatin 1.1

Bacteria May Cope Differently from Similar Membrane Damage Caused by the Australian Tree Frog Antimicrobial Peptide Maculatin 1.1

Multimerization of a Proline-Rich Antimicrobial Peptide, Chex-Arg20, Alters Its Mechanism of Interaction with the Escherichia coli Membrane

Melittin peptides exhibit different activity on different cells and model membranes

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