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Membrane activity of biomimetic facially amphiphilic antibiotics

Journal of Physical Chemistry B, ISSN: 1520-6106, Vol: 110, Issue: 8, Page: 3527-3532
2006
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Article Description

Membranes are a central feature of all biological systems, and their ability to control many cellular processes is critically important. As a result, a better understanding of how molecules bind to and select between biological membranes is an active area of research. Antimicrobial host defense peptides are known to be membraneactive and, in many cases, exhibit discrimination between prokaryotic and eukaryotic cells. The design of synthetic molecules that capture the biological activity of these natural peptides has been shown. In this report, the interaction between our biomimetic structures and different biological membranes is reported using both model vesicle and in vitro bacterial cell experiments. Compound 1 induces 12% leakage at 20 μg/mL against phosphatidylglycerol (PG) - phosphatidylethanolamine (PE) vesicles vs only 3% leakage at 200 μg/ mL against phosphatidyl-L-serine (PS)-phosphatidylcholine (PC) vesicles. Similarly, a 40% reduction in fluorescence is measured in lipid movement experiments for PG-PE compared to 10% for PS-PC at 600 s. A 30°C increase in the phase transition of stearoyl-oleoyl-phosphatidylserine is observed in the presence of 1. These results show that lipid composition is more important for selectivity than overall net charge. Additionally, the overall concentration of a given lipid is another important factor. An effort is made to connect model vesicle studies with in vitro data and naturally occurring lipid compositions. © 2006 American Chemical Society.

Bibliographic Details

Arnt, Lachelle; Rennie, Jason R; Linser, Sebastian; Willumeit, Regine; Tew, Gregory N

American Chemical Society (ACS)

Chemistry; Materials Science

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