ArticleScientific reports2019
Minor sequence modifications in temporin B cause drastic changes in antibacterial potency and selectivity by fundamentally altering membrane activity.
Article in Scientific reports, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 21 papers.
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Who cites it
21 citing papers in PubMed, 35 citations in OpenAlex.
- Chemical Optimization of Temporin A-L Peptides: From Native Isoforms to Enhanced Antimicrobial Analogs.ChemMedChem · 2026Review
- Early maturation of host antimicrobial peptide defences is associated with host-pathogen coexistence.Nature chemical biology · 2026Article
- The antibacterial activity and therapeutic potential of the amphibian-derived peptide TB_KKG6K.mSphere · 2025Article
- Carboxy-Amidated AamAP1-Lys has Superior Conformational Flexibility and Accelerated Killing of Gram-Negative Bacteria.Biochemistry · 2025Article
- Article
- QSAR Reveals Decreased Lipophilicity of Polar Residues Determines the Selectivity of Antimicrobial Peptide Activity.ACS omega · 2024Article
- Tryptophan End-Tagging Confers Antifungal Activity on a Tick-Derived Peptide by Triggering Reactive Oxygen Species Production.ACS omega · 2024Article
- Mechanistic Insight into the Early Stages of Toroidal Pore Formation by the Antimicrobial Peptide Smp24.Pharmaceutics · 2023Article
- Bolaamphiphile Analogues of 12-bis-THA ClmSphere · 2023Article
- Synergy between Winter Flounder antimicrobial peptides.npj antimicrobials and resistance · 2023Article
- Article
- Temporin B Forms Hetero-Oligomers with Temporin L, Modifies Its Membrane Activity, and Increases the Cooperativity of Its Antibacterial Pharmacodynamic Profile.Biochemistry · 2022Article
- In Vitro & In Vivo Studies on Identifying and Designing Temporin-1CEh from the Skin Secretion ofPharmaceutics · 2022Article
- Multiple Antimicrobial Effects of Hybrid Peptides Synthesized Based on the Sequence of Ribosomal S1 Protein fromInternational journal of molecular sciences · 2022Article
- New Perspectives in the Antimicrobial Activity of the Amphibian Temporin B: Peptide Analogs Are Effective Inhibitors ofJournal of fungi (Basel, Switzerland) · 2021Article
- Therapeutic Potential of Antimicrobial Peptides in Polymicrobial Biofilm-Associated Infections.International journal of molecular sciences · 2021Review
- The Antimicrobial Peptide Temporin G: Anti-Biofilm, Anti-Persister Activities, and Potentiator Effect of Tobramycin Efficacy AgainstInternational journal of molecular sciences · 2020Article
- Design, Engineering and Discovery of Novel α-Helical and β-Boomerang Antimicrobial Peptides against Drug Resistant Bacteria.International journal of molecular sciences · 2020Review
- Synthetic Antimicrobial Peptide Tuning Permits Membrane Disruption and Interpeptide Synergy.ACS pharmacology & translational science · 2020Article
- Temporin L and aurein 2.5 have identical conformations but subtly distinct membrane and antibacterial activities.Scientific reports · 2019Article
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Authors and funding
13 authors at 4 institutions in 2 countries.
Funding
Abstract
Antimicrobial peptides (AMPs) are a potential source of new molecules to counter the increase in antimicrobial resistant infections but a better understanding of their properties is required to understand their native function and for effective translation as therapeutics. Details of the mechanism of their interaction with the bacterial plasma membrane are desired since damage or penetration of this structure is considered essential for AMPs activity. Relatively modest modifications to AMPs primary sequence can induce substantial changes in potency and/or spectrum of activity but, hitherto, have not been predicted to substantially alter the mechanism of interaction with the bacterial plasma membrane. Here we use a combination of molecular dynamics simulations, circular dichroism, solid-state NMR and patch clamp to investigate the extent to which temporin B and its analogues can be distinguished both in vitro and in silico on the basis of their interactions with model membranes. Enhancing the hydrophobicity of the N-terminus and cationicity of the C-terminus in temporin B improves its membrane activity and potency against both Gram-negative and Gram-positive bacteria. In contrast, enhancing the cationicity of the N-terminus abrogates its ability to trigger channel conductance and renders it ineffective against Gram-positive bacteria while nevertheless enhancing its potency against Escherichia coli. Our findings suggest even closely related AMPs may target the same bacterium with fundamentally differing mechanisms of action.
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Registered trials
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