ArticleThe Journal of biological chemistry2015
Bacteria May Cope Differently from Similar Membrane Damage Caused by the Australian Tree Frog Antimicrobial Peptide Maculatin 1.1.
Article in The Journal of biological chemistry, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 29 papers.
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Who cites it
29 citing papers in PubMed, 64 citations in OpenAlex.
- Lipidomic Profile Reconstruction of Therapeutic Membrane Targets Using Physics-Based Optimization with Limited Activity Data.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2026Article
- Bacterial cell fate under stress: lipid remodeling and antimicrobial peptide attack.npj antimicrobials and resistance · 2026Article
- Frog Skin Peptides: Nature's Dual-Action Weapons Against Infection and Cancer.Antibiotics (Basel, Switzerland) · 2026Review
- Membrane selectivity and pore formation of SprA1 and SprA2 hemolytic peptides from Staphylococcus aureus type I toxin-antitoxin systems.The FEBS journal · 2025Article
- Article
- Lipid Shape as a Membrane Activity Modulator of a Fusogenic Antimicrobial Peptide.Journal of chemical information and modeling · 2025Article
- Selective Optical Imaging for Detection of Bacterial Biofilms in Tissues.Journal of imaging · 2023Article
- Review: Structure-Activity Relationship of Antimicrobial Peptoids.Pharmaceutics · 2023Review
- Advancements in antimicrobial nanoscale materials and self-assembling systems.Chemical Society reviews · 2022Review
- Caerin 1 Peptides, the Potential Jack-of-All-Trades for the Multiple Antibiotic-Resistant Bacterial Infection Treatment and Cancer Immunotherapy.BioMed research international · 2022Review
- Role of lipopolysaccharide in antimicrobial and cell penetrating peptide membrane interactions probed by deuterium NMR of whole cells.BBA advances · 2022Article
- In-cell DNP NMR reveals multiple targeting effect of antimicrobial peptide.Journal of structural biology: X · 2022Article
- Bioactive cationic peptides as potential agents for breast cancer treatment.Bioscience reports · 2021Article
- Conformation and membrane interaction studies of the potent antimicrobial and anticancer peptide palustrin-Ca.Scientific reports · 2021Article
- Host Defense Peptides: Dual Antimicrobial and Immunomodulatory Action.International journal of molecular sciences · 2021Review
- C-terminus amidation influences biological activity and membrane interaction of maculatin 1.1.Amino acids · 2021Article
- Membrane-Targeting Triphenylphosphonium Functionalized Ciprofloxacin for Methicillin-Resistant Staphylococcus aureus (MRSA).Antibiotics (Basel, Switzerland) · 2020Article
- A Novel Antimicrobial Peptide (Kassinatuerin-3) Isolated from the Skin Secretion of the African Frog,Biology · 2020Article
- The Location of the Antimicrobial Peptide Maculatin 1.1 in Model Bacterial Membranes.Frontiers in chemistry · 2020Article
- Mode-of-Action of Antimicrobial Peptides: Membrane Disruption vs. Intracellular Mechanisms.Frontiers in medical technology · 2020Review
Corrections and comments
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Authors and funding
4 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Maculatin 1.1 (Mac1) is an antimicrobial peptide from the skin of Australian tree frogs and is known to possess selectivity toward Gram-positive bacteria. Although Mac1 has membrane disrupting activity, it is not known how Mac1 selectively targets Gram-positive over Gram-negative bacteria. The interaction of Mac1 with Escherichia coli, Staphylococcus aureus, and human red blood cells (hRBC) and with their mimetic model membranes is here reported. The peptide showed a 16-fold greater growth inhibition activity against S. aureus (4 μM) than against E. coli (64 μM) and an intermediate cytotoxicity against hRBC (30 μM). Surprisingly, Sytox Green uptake monitored by flow cytometry showed that Mac1 compromised both bacterial membranes with similar efficiency at ∼20-fold lower concentration than the reported minimum inhibition concentration against S. aureus. Mac1 also reduced the negative potential of S. aureus and E. coli membrane with similar efficacy. Furthermore, liposomes mimicking the cell membrane of S. aureus (POPG/TOCL) and E. coli (POPE/POPG) were lysed at similar concentrations, whereas hRBC-like vesicles (POPC/SM/Chol) remained mostly intact in the presence of Mac1. Remarkably, when POPG/TOCL and POPE/POPG liposomes were co-incubated, Mac1 did not induce leakage from POPE/POPG liposomes, suggesting a preference toward POPG/TOCL membranes that was supported by surface plasma resonance assays. Interestingly, circular dichroism spectroscopy showed a similar helical conformation in the presence of the anionic liposomes but not the hRBC mimics. Overall, the study showed that Mac1 disrupts bacterial membranes in a similar fashion before cell death events and would preferentially target S. aureus over E. coli or hRBC membranes.
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