CPPs are short peptide sequences with translocation capacity across the biomembrane.
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Non-enzymatic lipid peroxidation may change biomembrane structure and function.
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Understanding drug-biomembrane interactions at high resolution is a key issue in current biophysical and pharmaceutical research.
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We hope this study regarding technique optimization will prompt the advancement of biomembrane-camouflaged nanoparticles as a newly emerging biomimetic technology.
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Lipid molecules, structural components of biomembranes, have been proposed for an important role in membrane fusion.
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Although biomembranes are targets for reactive oxygen species attack, little is known about the role of their specific interactions.
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This method allows for the presentation of tethered, laterally mobile biomembranes in three dimensions with functionally embedded attachment peptides for mobile ligand displays.
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Members of the major facilitator superfamily (MFS) of transport proteins are essential for the movement of a wide range of substrates across biomembranes.
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Here we used real-time atomic force microscopy (AFM) imaging to visualize the interaction of the antibiotic azithromycin with lipid domains in model biomembranes.