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

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    Type
    Article
    Authors
    Rydberg, Hanna A
    Kunze, Angelika
    Carlsson, Nils
    Altgärde, Noomi
    Svedhem, Sofia
    Nordén, Bengt
    Date
    2014-04-18
    Online Publication Date
    2014-04-18
    Print Publication Date
    2014-07
    Permanent link to this record
    http://hdl.handle.net/10754/596807
    
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    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.
    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.
    Publisher
    Springer Nature
    Journal
    European Biophysics Journal
    DOI
    10.1007/s00249-014-0958-9
    PubMed ID
    24743917
    PubMed Central ID
    PMC4053608
    ae974a485f413a2113503eed53cd6c53
    10.1007/s00249-014-0958-9
    Scopus Count
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