Research on lipid/drug interactions at the nanoscale underpins the emergence of synergistic mechanisms for topical drug administration. The structural understanding of bio-mimetic systems employing 1,2-dipalmitoyl-sn-glycero-3-phosphocholine (DPPC) as a lung surfactant model mixed with antibiotics, as well as their biophysical properties, is of critical importance to modulate the effectiveness of therapeutic agents released directly to the airways. In this paper, we investigate the structural details of the interaction between Levofloxacin, 'a respiratory quinolone', and the macrolide Clarithromycin, with DPPC monolayers at the air-water interface, using a combination of Brewster angle microscopy, polarization modulation-infrared reflection-adsorption spectroscopy (PM-IRRAS), surface pressure isotherms and neutron reflectometry (NR) to describe the structural details of this interaction. The results allowed association of changes in the π-A isotherm profile with changes in the molecular organization and the co-localization of the antibiotics within the lipid monolayer by NR measurements. Overall, both antibiotics are able to increase the thickness of the acyl tails in DPPC monolayers with a corresponding reduction in tail tilt as well as to interact with the phospholipid headgroups as shown by PM-IRRAS experiments. The effects on the DPPC monolayers are correlated with the physical-chemical properties of each antibiotic and dependent on its concentration.
Download full-text PDF |
Source |
|---|---|
| http://dx.doi.org/10.1016/j.bbamem.2019.05.016 | DOI Listing |
Publication Analysis
Top Keywords
Similar Publications
Incorporation of Triacylglycerol and Cholesteryl Ester Droplets in Phase-Separated Giant Unilamellar Vesicles.
Langmuir
March 2025
Research Center for Macromolecules and Biomaterials, National Institute for Materials Science, 1-1 Namiki, Tsukuba, Ibaraki 305-0044, Japan.
Cytoplasmic lipid droplets form from the endoplasmic reticulum (ER). Because the ER membrane can undergo phase separation, the interaction of lipid droplets with phase-separated bilayers is of significant interest. In this study, we used fluorescence microscopy to investigate the incorporation of droplets composed of triolein, trilinolein, trimyristolein, trieicosenoin, and cholesteryl arachidonate in the bilayers of giant unilamellar vesicles (GUVs) consisting of a mixture of 1,2-dioleoyl--glycero-3-phosphocholine (DOPC), 1,2-dipalmitoyl--glycero-3-phosphocholine (DPPC), and cholesterol.
View Article and Find Full Text PDFVitamin E Acetate Causes Softening of Pulmonary Surfactant Membrane Models.
Chem Res Toxicol
February 2025
Department of Chemistry and Biochemistry, University of Windsor, Windsor, ON N9B 3P4, Canada.
The popularity of electronic cigarettes and vaping products has launched the outbreak of a condition affecting the respiratory system of users, known as electronic-cigarette/vaping-associated lung injury (EVALI). The build-up of vitamin E acetate (VEA), a diluent of some illicit vaping oils, in the bronchoalveolar lavage of patients with EVALI provided circumstantial evidence as a target for investigation. In this work, we provide a fundamental characterization of the interaction of VEA with lung cells and pulmonary surfactant (PS) models to explore the mechanisms by which vaping-related lung injuries may be present.
View Article and Find Full Text PDFWhey-Derived Antimicrobial Anionic Peptide Interaction with Model Membranes and Cells.
Langmuir
January 2025
Departamento de Química, Catedra de Química Biológica, Facultad de Ciencias Exactas, Físicas y Naturales, Universidad Nacional de Córdoba, Córdoba 5000, Argentina.
The present work focuses on one of the possible target mechanisms of action of the anionic antimicrobial peptide β-lg derived from trypsin hydrolysis of β-lactoglobulin. After confirmation of bactericidal activity against a pathogenic Gram(+) strain and demonstration of the innocuousness on a eukaryotic cell line, we investigated the interaction of β-lg with monolayers and bilayers of dpPC and dpPC:dpPG as model membranes of eukaryotic and bacterial membranes, respectively. In monolayers, compared to zwitterionic dpPC, in the negatively charged dpPC-dpPG, β-lg injected into the subphase penetrated up to higher surface pressures and showed greater extents of penetration with increasing concentration in the subphase.
View Article and Find Full Text PDFDifferential insertion of arginine in saturated and unsaturated lipid vesicles.
Biochim Biophys Acta Biomembr
December 2024
Applied Biophysics and Food Research Center (Centro de Investigaciones en Biofísica Aplicada y Alimentos, CIBAAL, National University of Santiago del Estero and CONICET), RN 9 - Km 1125, 4206 Santiago del Estero, Argentina. Electronic address:
Article Synopsis
- This study investigates how L-Arginine (L-Arg) affects lipid membranes using various techniques like fluorescence spectroscopy and dynamic light scattering.
- L-Arg reduces the polarizability of saturated lipids, leading to an increase in vesicle size, while in unsaturated lipids, it increases polarizability without significantly changing size.
- The interaction of L-Arg differs based on whether the lipids are saturated or unsaturated, and cholesterol appears to dampen these effects.
The Interactions of Anti-HIV Pronucleotides with a Model Phospholipid Membrane.
Molecules
December 2024
Institute of Chemical Technology and Engineering, Poznan University of Technology, Berdychowo 4, 60-965 Poznań, Poland.
Pronucleotides, after entering the cell, undergo chemical or enzymatic conversion into nucleotides with a free phosphate residue, and the released nucleoside 5'-monophosphate is then phosphorylated to the biologically active form, namely nucleoside 5'-triphosphate. The active form can inhibit HIV virus replication. For the most effective therapy, it is necessary to improve the transport of prodrugs into organelles.
View Article and Find Full Text PDFWant AI Summaries of new PubMed Abstracts delivered to your In-box?
Enter search terms and have AI summaries delivered each week - change queries or unsubscribe any time!