ArticleBiophysical journal2004
Interaction of melittin with membrane cholesterol: a fluorescence approach.
Article in Biophysical journal, 2004. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 40 papers.
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Who cites it
40 citing papers in PubMed, 122 citations in OpenAlex.
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- Charge, Hydrophobicity, and Lipid Type Drive Antimicrobial Peptides' Unique Perturbation Ensembles.Biochemistry · 2025Article
- Insights into the Adsorption Mechanisms of the Antimicrobial Peptide CIDEM-501 on Membrane Models.Antibiotics (Basel, Switzerland) · 2024Article
- The Functionality of Membrane-Inserting Proteins and Peptides: Curvature Sensing, Generation, and Pore Formation.The Journal of membrane biology · 2023Review
- Impacts of Hydrophobic Mismatch on Antimicrobial Peptide Efficacy and Bilayer Permeabilization.Antibiotics (Basel, Switzerland) · 2023Article
- Applications of fluorescence spectroscopy in protein conformational changes and intermolecular contacts.BBA advances · 2023Article
- Possible Role of Bent Structure of Methylated Lithocholic Acid on Artificial and Plasma Membranes.Membranes · 2022Article
- Measuring Membrane Penetration Depths and Conformational Changes in Membrane Peptides and Proteins.The Journal of membrane biology · 2022Review
- Membrane Cholesterol Content and Lipid Organization Influence Melittin and Pneumolysin Pore-Forming Activity.Toxins · 2022Article
- Site-directed fluorescence approaches to monitor the structural dynamics of proteins using intrinsic Trp and labeled with extrinsic fluorophores.STAR protocols · 2022Article
- Behaviour and interactions of proteins and peptides with and within membranes; from simple models to cellular membranes: general discussion.Faraday discussions · 2021Article
- Lack of Environmental Sensitivity of a Naturally Occurring Fluorescent Analog of Cholesterol.Journal of fluorescence · 2021Article
- Gating-related Structural Dynamics of the MgtE Magnesium Channel in Membrane-Mimetics Utilizing Site-Directed Tryptophan Fluorescence.Journal of molecular biology · 2021Article
- Hyaluronic Acid Coating Reduces the Leakage of Melittin Encapsulated in Liposomes and Increases Targeted Delivery to Melanoma Cells.Pharmaceutics · 2021Article
- Preliminary Characterization of NP339, a Novel Polyarginine Peptide with Broad Antifungal Activity.Antimicrobial agents and chemotherapy · 2021Article
- Localization Preference of Antimicrobial Peptides on Liquid-Disordered Membrane Domains.Frontiers in cell and developmental biology · 2020Article
- Biochemical and biophysical characterization of a prokaryotic MgProtein expression and purification · 2019Article
- Site-Directed Fluorescence Approaches for Dynamic Structural Biology of Membrane Peptides and Proteins.Frontiers in molecular biosciences · 2019Review
- Niosomes, an alternative for liposomal delivery.PloS one · 2018Article
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
We have monitored the organization and dynamics of the hemolytic peptide melittin in membranes containing cholesterol by utilizing the intrinsic fluorescence properties of its functionally important sole tryptophan residue and circular dichroism spectroscopy. The significance of this study is based on the fact that the natural target for melittin is the erythrocyte membrane, which contains high amounts of cholesterol. Our results show that the presence of cholesterol inhibits melittin-induced leakage of lipid vesicles and the extent of inhibition appears to be dependent on the concentration of membrane cholesterol. The presence of cholesterol is also shown to reduce binding of melittin to membranes. Our results show that fluorescence parameters such as intensity, emission maximum, and lifetime of membrane-bound melittin indicate a change in polarity in the immediate vicinity of the tryptophan residue probably due to increased water penetration in presence of cholesterol. This is supported by results from fluorescence quenching experiments using acrylamide as the quencher. Membrane penetration depth analysis by the parallax method shows that the melittin tryptophan is localized at a relatively shallow depth in membranes containing cholesterol. Analysis of energy transfer results using melittin tryptophan (donor) and dehydroergosterol (acceptor) indicates that dehydroergosterol is not randomly distributed and is preferentially localized around the tryptophan residue of membrane-bound melittin, even at the low concentrations used. Taken together, our results are relevant in understanding the interaction of melittin with membranes in general, and with cholesterol-containing membranes in particular, with possible relevance to its interaction with the erythrocyte membrane.
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