Vis enkel innførsel

dc.contributor.authorRekdal, Øystein
dc.contributor.authorHaug, Bengt Erik
dc.contributor.authorKalaaji, manar
dc.contributor.authorHunter, Howard N.
dc.contributor.authorLindin, Inger
dc.contributor.authorIsraelsson, Ingrid
dc.contributor.authorSolstad, Terese
dc.contributor.authorYang, Nannan
dc.contributor.authorBrandl, Martin
dc.contributor.authorMantzilas, Dimitrios
dc.contributor.authorVogel, Hans J.
dc.date.accessioned2022-05-16T09:27:49Z
dc.date.available2022-05-16T09:27:49Z
dc.date.issued2011-11-04
dc.description.abstractBackground: 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.citationRekdal 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):233-244en_US
dc.identifier.cristinIDFRIDAID 867573
dc.identifier.doi10.1074/jbc.M111.279281
dc.identifier.issn0021-9258
dc.identifier.issn1083-351X
dc.identifier.urihttps://hdl.handle.net/10037/25136
dc.language.isoengen_US
dc.publisherElsevieren_US
dc.relation.journalJournal of Biological Chemistry
dc.rights.accessRightsopenAccessen_US
dc.rights.holderCopyright 2012 The American Society for Biochemistry and Molecular Biology, Incen_US
dc.subjectVDP::Medisinske fag: 700::Basale medisinske, odontologiske og veterinærmedisinske fag: 710::Medisinsk biokjemi: 726en_US
dc.subjectVDP::Midical sciences: 700::Basic medical, dental and veterinary sciences: 710::Medical biochemistry: 726en_US
dc.titleThe relative spatial positions of tryptophan and cationic residues in helical membrane-active peptides determines their cytotoxicityen_US
dc.type.versionpublishedVersionen_US
dc.typeJournal articleen_US
dc.typeTidsskriftartikkelen_US
dc.typePeer revieweden_US


Tilhørende fil(er)

Thumbnail

Denne innførselen finnes i følgende samling(er)

Vis enkel innførsel