Membrane interaction and secondary structure of de novo designed arginine-and tryptophan peptides with dual function
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AbstractCell-penetrating peptides and antimicrobial peptides are two classes of positively charged membrane active peptides with several properties in common. The challenge is to combine knowledge about the membrane interaction mechanisms and structural properties of the two classes to design peptides with membrane-specific actions, useful either as transporters of cargo or as antibacterial substances. Membrane active peptides are commonly rich in arginine and tryptophan. We have previously designed a series of arg/trp peptides and investigated how the position and number of tryptophans affect cellular uptake. Here we explore the antimicrobial properties and the interaction with lipid model membranes of these peptides, using minimal inhibitory concentrations assay (MIC), circular dichroism (CD) and linear dichroism (LD). The results show that the arg/trp peptides inhibit the growth of the two gram positive strains Staphylococcus aureus and Staphylococcus pyogenes, with some individual variations depending on the position of the tryptophans. No inhibition of the gram negative strains Proteus mirabilis or Pseudomonas aeruginosa was noticed. CD indicated that when bound to lipid vesicles one of the peptides forms an α-helical like structure, whereas the other five exhibited rather random coiled structures. LD indicated that all six peptides were somehow aligned parallel with the membrane surface. Our results do not reveal any obvious connection between membrane interaction and antimicrobial effect for the studied peptides. By contrast cell-penetrating properties can be coupled to both the secondary structure and the degree of order of the peptides. © 2012 Elsevier Inc.
CitationRydberg HA, Carlsson N, Nordén B (2012) Membrane interaction and secondary structure of de novo designed arginine-and tryptophan peptides with dual function. Biochemical and Biophysical Research Communications 427: 261–265. Available: http://dx.doi.org/10.1016/j.bbrc.2012.09.030.
SponsorsThis work was supported by an award to B.N. from the King Abdullah University of Science and Technology (KAUST). We thank Professor Lars Ohrstrom and Gabriella Lindberg for help performing the MIC tests.
CollectionsPublications Acknowledging KAUST Support
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