dc.contributor.author | Rekdal, Øystein | |
dc.contributor.author | Haug, Bengt Erik | |
dc.contributor.author | Kalaaji, manar | |
dc.contributor.author | Hunter, Howard N. | |
dc.contributor.author | Lindin, Inger | |
dc.contributor.author | Israelsson, Ingrid | |
dc.contributor.author | Solstad, Terese | |
dc.contributor.author | Yang, Nannan | |
dc.contributor.author | Brandl, Martin | |
dc.contributor.author | Mantzilas, Dimitrios | |
dc.contributor.author | Vogel, Hans J. | |
dc.date.accessioned | 2022-05-16T09:27:49Z | |
dc.date.available | 2022-05-16T09:27:49Z | |
dc.date.issued | 2011-11-04 | |
dc.description.abstract | Background: Tryptophan side chains can influence the binding of amphipathic peptides to biological membranes.
<p>Results: The cytotoxic activity of model helical amphipathic peptides was markedly influenced by the positions of tryptophan
residues in the sequence.
<p>Conclusion: Tryptophan residues located adjacent to a hydrophobic helical portion created the most potent cytotoxic peptides.
<p>Significance: More potent anticancer helical peptides can now be designed. | en_US |
dc.identifier.citation | Rekdal Ø, Haug BE, Kalaaji m, Hunter, Lindin i, Israelsson i, Solstad T, Yang N, Brandl mb, Mantzilas DM, Vogel. The relative spatial positions of tryptophan and cationic residues in helical membrane-active peptides determines their cytotoxicity. Journal of Biological Chemistry. 2012;287(1):233-244 | en_US |
dc.identifier.cristinID | FRIDAID 867573 | |
dc.identifier.doi | 10.1074/jbc.M111.279281 | |
dc.identifier.issn | 0021-9258 | |
dc.identifier.issn | 1083-351X | |
dc.identifier.uri | https://hdl.handle.net/10037/25136 | |
dc.language.iso | eng | en_US |
dc.publisher | Elsevier | en_US |
dc.relation.journal | Journal of Biological Chemistry | |
dc.rights.accessRights | openAccess | en_US |
dc.rights.holder | Copyright 2012 The American Society for Biochemistry and Molecular Biology, Inc | en_US |
dc.subject | VDP::Medisinske fag: 700::Basale medisinske, odontologiske og veterinærmedisinske fag: 710::Medisinsk biokjemi: 726 | en_US |
dc.subject | VDP::Midical sciences: 700::Basic medical, dental and veterinary sciences: 710::Medical biochemistry: 726 | en_US |
dc.title | The relative spatial positions of tryptophan and cationic residues in helical membrane-active peptides determines their cytotoxicity | en_US |
dc.type.version | publishedVersion | en_US |
dc.type | Journal article | en_US |
dc.type | Tidsskriftartikkel | en_US |
dc.type | Peer reviewed | en_US |