ArticleBiophysical journal2016
Membrane Binding and Oligomerization of the Lipopeptide A54145 Studied by Pyrene Fluorescence.
Article in Biophysical journal, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.
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Who cites it
12 citing papers in PubMed.
- Novel Synthetic Strategies Towards Analogues of Cadaside and Malacidin Antibiotic Peptides.Biomolecules · 2025Article
- State of the Art of Cyclic Lipopeptide-Membrane Interactions: Pore Formation and Bilayer Permeability.Pharmaceutics · 2025Review
- Synergy Mechanisms of Daptomycin-Fosfomycin Combinations in Daptomycin-Susceptible and -Resistant Methicillin-Resistant Staphylococcus aureus:Antimicrobial agents and chemotherapy · 2022Article
- 2- and 2,7-Substituted para-N-Methylpyridinium Pyrenes: Syntheses, Molecular and Electronic Structures, Photophysical, Electrochemical, and Spectroelectrochemical Properties and Binding to Double-Stranded (ds) DNA.Chemistry (Weinheim an der Bergstrasse, Germany) · 2021Article
- The Antibiotic Peptide Daptomycin Functions by Reorganizing the Membrane.The Journal of membrane biology · 2021Review
- Review
- Synthesis, Photophysical and Electronic Properties of New Red-to-NIR Emitting Donor-Acceptor Pyrene Derivatives.Chemistry (Weinheim an der Bergstrasse, Germany) · 2020Article
- Controllable fluorescenceRSC advances · 2019Article
- The calcium-dependent lipopeptide antibiotics: structure, mechanism, & medicinal chemistry.MedChemComm · 2019Review
- Cadasides, Calcium-Dependent Acidic Lipopeptides from the Soil Metagenome That Are Active against Multidrug-Resistant Bacteria.Journal of the American Chemical Society · 2019Article
- Culture-independent discovery of the malacidins as calcium-dependent antibiotics with activity against multidrug-resistant Gram-positive pathogens.Nature microbiology · 2018Article
- Daptomycin-Phosphatidylglycerol Domains in Lipid Membranes.Langmuir : the ACS journal of surfaces and colloids · 2017Article
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Authors and funding
4 authors.
Funding
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Abstract
A54145 is a lipopeptide antibiotic related to daptomycin that permeabilizes bacterial cell membranes. Its action requires both calcium and phosphatidylglycerol in the target membrane, and it is accompanied by the formation of membrane-associated oligomers. We here probed the interaction of A54145 with model membranes composed of dimyristoylphosphatidylcholine and dimyristoylphosphatidylglycerol, using the steady-state and time-resolved fluorescence of a pyrene-labeled derivative (Py-A54145). In solution, the labeled peptide was found to exist as a monomer. Its membrane interaction occurred in two stages that could be clearly distinguished by varying the calcium concentration. In the first stage, which was observed between 0.15 and 1 mM calcium, Py-A54145 bound to the membrane, as indicated by a strong increase in pyrene monomer emission. At the same calcium concentration, excimer emission increased also, suggesting that Py-A54145 had oligomerized. A global analysis of the time-resolved pyrene monomer and excimer fluorescence confirmed that Py-A54145 forms oligomers quantitatively and concomitantly with membrane binding. When calcium was raised beyond 1 mM, a distinct second transition was observed that may correspond to a doubling of the number of oligomer subunits. The collective findings confirm and extend our understanding of the action mode of A54145 and daptomycin.
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