Modulation of lipid membrane structural and mechanical properties by a peptidomimetic derived from reduced amide scaffold
Biochimica et Biophysica Acta (BBA) - Biomembranes, ISSN: 0005-2736, Vol: 1859, Issue: 5, Page: 734-744
2017
- 19Citations
- 26Captures
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Example: if you select the 1-year option for an article published in 2019 and a metric category shows 90%, that means that the article or review is performing better than 90% of the other articles/reviews published in that journal in 2019. If you select the 3-year option for the same article published in 2019 and the metric category shows 90%, that means that the article or review is performing better than 90% of the other articles/reviews published in that journal in 2019, 2018 and 2017.
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Metrics Details
- Citations19
- Citation Indexes19
- 19
- CrossRef8
- Captures26
- Readers26
- 26
Article Description
Understanding how antimicrobial peptidomimetics interact with lipid membranes is important in battling multidrug resistant bacterial pathogens. We study the effects of a recently reported peptidomimetic on lipid bilayer structural and mechanical properties. The compound referred to as E107-3 is synthesized based on the acylated reduced amide scaffold and has been shown to exhibit good antimicrobial potency. Our vesicle leakage assay indicates that the compound increases lipid bilayer permeability. We use micropipette aspiration to explore the kinetic response of giant unilamellar vesicles (GUVs). Exposure to the compound causes the GUV protrusion length L P to spontaneously increase and then decrease, followed by GUV rupture. Solution atomic force microscopy (AFM) is used to visualize lipid bilayer structural modulation within a nanoscopic regime. Unlike melittin, which produces pore-like structures, the peptidomimetic compound is found to induce nanoscopic heterogeneous structures. Finally, we use AFM-based force spectroscopy to study the impact of the compound on lipid bilayer mechanical properties. We find that incremental addition of the compound to planar lipid bilayers results in a moderate decrease of the bilayer puncture force F P and a 39% decrease of the bilayer area compressibility modulus K A. To explain our experimental data, we propose a membrane interaction model encompassing disruption of lipid chain packing and extraction of lipid molecules. The later action mode is supported by our observation of a double-bilayer structure in the presence of fusogenic calcium ions.
Bibliographic Details
http://www.sciencedirect.com/science/article/pii/S0005273617300342; http://dx.doi.org/10.1016/j.bbamem.2017.01.026; http://www.scopus.com/inward/record.url?partnerID=HzOxMe3b&scp=85011807480&origin=inward; http://www.ncbi.nlm.nih.gov/pubmed/28132901; https://linkinghub.elsevier.com/retrieve/pii/S0005273617300342; https://dx.doi.org/10.1016/j.bbamem.2017.01.026
Elsevier BV
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