Peptide-membrane interactions of arginine-tryptophan peptides probed using quartz crystal microbalance with dissipation monitoring.
Online Publication Date2014-04-18
Print Publication Date2014-07
Permanent link to this recordhttp://hdl.handle.net/10754/596807
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AbstractMembrane-active peptides include peptides that can cross cellular membranes and deliver macromolecular cargo as well as peptides that inhibit bacterial growth. Some of these peptides can act as both transporters and antibacterial agents. It is desirable to combine the knowledge from these two different fields of membrane-active peptides into design of new peptides with tailored actions, as transporters of cargo or as antibacterial substances, targeting specific membranes. We have previously shown that the position of the amino acid tryptophan in the peptide sequence of three arginine-tryptophan peptides affects their uptake and intracellular localization in live mammalian cells, as well as their ability to inhibit bacterial growth. Here, we use quartz crystal microbalance with dissipation monitoring to assess the induced changes caused by binding of the three peptides to supported model membranes composed of POPC, POPC/POPG, POPC/POPG/cholesterol or POPC/lactosyl PE. Our results indicate that the tryptophan position in the peptide sequence affects the way these peptides interact with the different model membranes and that the presence of cholesterol in particular seems to affect the membrane interaction of the peptide with an even distribution of tryptophans in the peptide sequence. These results give mechanistic insight into the function of these peptides and may aid in the design of membrane-active peptides with specified cellular targets and actions.
CitationRydberg HA, Kunze A, Carlsson N, Altgärde N, Svedhem S, et al. (2014) Peptide-membrane interactions of arginine-tryptophan peptides probed using quartz crystal microbalance with dissipation monitoring. Eur Biophys J 43: 241–253. Available: http://dx.doi.org/10.1007/s00249-014-0958-9.
SponsorsThis work was supported by an award to B.N. from the King Abdullah University of Science and Technology (KAUST). The research was pursued within the SUPRA Centre of Excellence supported by the Swedish Research Council.
JournalEuropean Biophysics Journal
PubMed Central IDPMC4053608
CollectionsPublications Acknowledging KAUST Support
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