ArticleBiophysical journal2011
Thermodynamic profiling of peptide membrane interactions by isothermal titration calorimetry: a search for pores and micelles.
Article in Biophysical journal, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 15 papers.
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Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
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Who cites it
15 citing papers in PubMed, 44 citations in OpenAlex.
- Physicochemical Characteristics of Amphipathic Peptides and Their Cytotoxic Effects on Cancer and Normal Cell Lines.International journal of molecular sciences · 2026Article
- Predicting peptide orientation in membrane interactions: a review on transmembrane and surface-bound states.European biophysics journal : EBJ · 2026Review
- Applications of Isothermal Titration Calorimetry in Studying Biomimetic Nanocarriers.Biomolecules · 2025Review
- The Functionality of Membrane-Inserting Proteins and Peptides: Curvature Sensing, Generation, and Pore Formation.The Journal of membrane biology · 2023Review
- Fever temperatures impair hemolysis caused by strains ofHeliyon · 2022Article
- Lipidation of Temporin-1CEb Derivatives as a Tool for Activity Improvement, Pros and Cons of the Approach.International journal of molecular sciences · 2021Article
- Double-Headed Cationic Lipopeptides: An Emerging Class of Antimicrobials.International journal of molecular sciences · 2020Article
- Revisiting the Interaction of Melittin with Phospholipid Bilayers: The Effects of Concentration and Ionic Strength.International journal of molecular sciences · 2020Article
- Unveiling the binding and orientation of the antimicrobial peptide Plantaricin 149 in zwitterionic and negatively charged membranes.European biophysics journal : EBJ · 2019Article
- Biophysical Investigations Elucidating the Mechanisms of Action of Antimicrobial Peptides and Their Synergism.Biomolecules · 2018Review
- Arginine-lysine positional swap of the LL-37 peptides reveals evolutional advantages of the native sequence and leads to bacterial probes.Biochimica et biophysica acta. Biomembranes · 2017Article
- Submillisecond Dynamics of Mastoparan X Insertion into Lipid Membranes.The journal of physical chemistry letters · 2016Article
- Pro-apoptotic Bax molecules densely populate the edges of membrane pores.Scientific reports · 2016Article
- In vivo evaluation of PEGylated ⁶⁴Cu-liposomes with theranostic and radiotherapeutic potential using micro PET/CT.European journal of nuclear medicine and molecular imaging · 2016Article
- Side chain hydrophobicity modulates therapeutic activity and membrane selectivity of antimicrobial peptide mastoparan-X.PloS one · 2014Article
Corrections and comments
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Authors and funding
2 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Antimicrobial peptides are known to interact strongly with negatively charged lipid membranes, initially by peripheral insertion of the peptide into the bilayer, which for some antimicrobial peptides will be followed by pore formation, and successive solubilization of the membranes resulting in mixed peptide-lipid micelles. We have investigated the mode of action of the antimicrobial peptide mastoparan-X using isothermal titration calorimetry (ITC) and cryo-transmission electron microscopy (cryo-TEM). The results show that mastoparan-X induces a range of structural transitions of POPC/POPG (3:1) lipid membranes at different peptide/lipid ratios. It has been established that ITC can be used as a fast method for localizing membrane transitions and when combined with DLS and cryo-TEM can elucidate structural changes, including the threshold for pore formation and micellation. Cryo-TEM was employed to confirm the structural changes associated with the thermodynamic transitions found by ITC. The pore-formation process has furthermore been investigated in detail and the thermodynamic parameters of pore formation have been characterized using a system-specific temperature where the enthalpy of peptide partitioning becomes zero (T(zero)). This allows for an exclusive study of the pore-formation process. The use of ITC to find T(zero) allows for characterization of the thermodynamic parameters of secondary processes on lipid membranes.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.