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dc.contributor.authorPaulsen, Victoria
dc.contributor.authorBlencke, Hans-Matti
dc.contributor.authorBenincasa, Monica
dc.contributor.authorHaug, Tor
dc.contributor.authorEksteen, Jacobus Johannes
dc.contributor.authorStyrvold, Olaf B.
dc.contributor.authorScocchi, Marco
dc.contributor.authorStensvåg, Klara
dc.date.accessioned2013-03-08T09:38:53Z
dc.date.available2013-03-08T09:38:53Z
dc.date.issued2012
dc.description.abstractArasin 1 is a 37 amino acid long proline-rich antimicrobial peptide isolated from the spider crab, Hyas araneus. In this work the active region of arasin 1 was identified through structure-activity studies using different peptide fragments derived from the arasin 1 sequence. The pharmacophore was found to be located in the proline/arginine-rich NH2 terminus of the peptide and the fragment arasin 1(1–23) was almost equally active to the full length peptide. Arasin 1 and its active fragment arasin 1(1–23) were shown to be non-toxic to human red blood cells and arasin 1(1–23) was able to bind chitin, a component of fungal cell walls and the crustacean shell. The mode of action of the fully active N-terminal arasin 1(1–23) was explored through killing kinetic and membrane permeabilization studies. At the minimal inhibitory concentration (MIC), arasin 1(1–23) was not bactericidal and had no membrane disruptive effect. In contrast, at concentrations of 5×MIC and above it was bactericidal and interfered with membrane integrity. We conclude that arasin 1(1–23) has a different mode of action than lytic peptides, like cecropin P1. Thus, we suggest a dual mode of action for arasin 1(1–23) involving membrane disruption at peptide concentrations above MIC, and an alternative mechanism of action, possibly involving intracellular targets, at MIC.en
dc.identifier.citationPLoS ONE (2012), vol. 8(1): e53326en
dc.identifier.cristinIDFRIDAID 966820
dc.identifier.doihttp://dx.doi.org/10.1371/journal.pone.0053326
dc.identifier.issn1932-6203
dc.identifier.urihttps://hdl.handle.net/10037/4925
dc.identifier.urnURN:NBN:no-uit_munin_4625
dc.language.isoengen
dc.publisherPublic Library of Science (PLoS)en
dc.rights.accessRightsopenAccess
dc.subjectVDP::Medical disciplines: 700::Basic medical, dental and veterinary science disciplines: 710::Medical molecular biology: 711en
dc.subjectVDP::Medisinske Fag: 700::Basale medisinske, odontologiske og veterinærmedisinske fag: 710::Medisinsk molekylærbiologi: 711en
dc.subjectVDP::Medical disciplines: 700::Basic medical, dental and veterinary science disciplines: 710::Medical microbiology: 715en
dc.subjectVDP::Medisinske Fag: 700::Basale medisinske, odontologiske og veterinærmedisinske fag: 710::Medisinsk mikrobiologi: 715en
dc.titleStructure-activity relationships of the antimicrobial peptide arasin 1 - and mode of action studies of the N terminal, proline-rich regionen
dc.typeJournal articleen
dc.typeTidsskriftartikkelen
dc.typePeer revieweden


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