Peptide-membrane interactions of arginine-tryptophan peptides probed using quartz crystal microbalance with dissipation monitoring.

Handle URI:
http://hdl.handle.net/10754/596807
Title:
Peptide-membrane interactions of arginine-tryptophan peptides probed using quartz crystal microbalance with dissipation monitoring.
Authors:
Rydberg, Hanna A; Kunze, Angelika; Carlsson, Nils; Altgärde, Noomi; Svedhem, Sofia; Nordén, Bengt
Abstract:
Membrane-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.
Citation:
Rydberg 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.
Publisher:
Springer Science + Business Media
Journal:
European Biophysics Journal
Issue Date:
18-Apr-2014
DOI:
10.1007/s00249-014-0958-9
PubMed ID:
24743917
PubMed Central ID:
PMC4053608
Type:
Article
ISSN:
0175-7571; 1432-1017
Sponsors:
This 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.
Appears in Collections:
Publications Acknowledging KAUST Support

Full metadata record

DC FieldValue Language
dc.contributor.authorRydberg, Hanna Aen
dc.contributor.authorKunze, Angelikaen
dc.contributor.authorCarlsson, Nilsen
dc.contributor.authorAltgärde, Noomien
dc.contributor.authorSvedhem, Sofiaen
dc.contributor.authorNordén, Bengten
dc.date.accessioned2016-02-21T08:51:04Zen
dc.date.available2016-02-21T08:51:04Zen
dc.date.issued2014-04-18en
dc.identifier.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.en
dc.identifier.issn0175-7571en
dc.identifier.issn1432-1017en
dc.identifier.pmid24743917en
dc.identifier.doi10.1007/s00249-014-0958-9en
dc.identifier.urihttp://hdl.handle.net/10754/596807en
dc.description.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.en
dc.description.sponsorshipThis 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.en
dc.publisherSpringer Science + Business Mediaen
dc.rightsThis article is distributed under the terms of the Creative Commons Attribution License which permits any use, distribution, and reproduction in any medium, provided the original author(s) and the source are credited.en
dc.subject.meshArginineen
dc.subject.meshTryptophanen
dc.subject.meshQuartz Crystal Microbalance Techniquesen
dc.titlePeptide-membrane interactions of arginine-tryptophan peptides probed using quartz crystal microbalance with dissipation monitoring.en
dc.typeArticleen
dc.identifier.journalEuropean Biophysics Journalen
dc.identifier.pmcidPMC4053608en
dc.contributor.institutionDepartment of Chemical and Biological Engineering, Chalmers University of Technology, Kemivägen 10, 412 96, Göteborg, Sweden.en
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