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dc.contributor.authorMoe, Morten Kaare
dc.contributor.authorHaug, Tor
dc.contributor.authorSydnes, Magne Olav
dc.contributor.authorSperstad, Sigmund
dc.contributor.authorLi, Chun
dc.contributor.authorVaagsfjord, Lena Christine
dc.contributor.authorde la Vega, Enrique
dc.contributor.authorStensvåg, Klara
dc.date.accessioned2019-01-17T09:12:03Z
dc.date.available2019-01-17T09:12:03Z
dc.date.issued2018-01-17
dc.description.abstractAs part of an ongoing exploration of marine invertebrates as a source of new antimicrobial peptides, hemocyte extracts from the red king crab, <i>Paralithodes camtschaticus</i>, were studied. Three cationic cysteine (Cys)-rich peptides, named paralithocins 1–3, were isolated by bioassay-guided purification, and their amino acid sequences determined by Edman degradation and expressed sequences tag analysis. Disulfide bond mapping was performed by high-resolution tandem mass spectrometry. The peptides (38–51 amino acids in length) share a unique Cys motif composed of eight Cys, forming four disulfide bridges with a bond connectivity of (Cys relative position) Cys1–Cys8, Cys2–Cys6, Cys3–Cys5, and Cys4–Cys7, a disulfide arrangement that has not been previously reported among antimicrobial peptides. Thus, paralithocins 1–3 may be assigned to a previously unknown family of antimicrobial peptides within the group of Cys-rich antimicrobial peptides. Although none of the isolated peptides displayed antimicrobial activity against the target strains <i>Escherichia coli, Pseudomonas aeruginosa</i>, or <i>Staphylococcus aureus</i>, they inhibited the growth of several marine bacterial strains with minimal inhibitory concentrations in the 12.5–100 μM range. These findings corroborate the hypothesis that marine organisms are a valuable source for discovering bioactive peptides with new structural motifs.en_US
dc.description.sponsorshipTromsø Research Foundation UiT The Arctic University of Norwayen_US
dc.descriptionSubmitted manuscript version. Published version available at <a href=https://doi.org/10.1021/acs.jnatprod.7b00780> https://doi.org/10.1021/acs.jnatprod.7b00780</a>. With permission from Moe, M.K., Haug, T., Sydnes, M.O., Sperstad, S.V., Li, C., Vaagsfjord, L.C., ... Stensvåg, K. (2018). Paralithocins, Antimicrobial Peptides with Unusual Disulfide Connectivity from the Red King Crab, <i>Paralithodes camtschaticus</i>. <i>Journal of natural products, 81</i>(1), 140-150. Copyright 2018 American Chemical Society.en_US
dc.identifier.citationMoe, M.K., Haug, T., Sydnes, M.O., Sperstad, S.V., Li, C., Vaagsfjord, L.C., ... Stensvåg, K. (2018). Paralithocins, Antimicrobial Peptides with Unusual Disulfide Connectivity from the Red King Crab, <i>Paralithodes camtschaticus</i>. <i>Journal of natural products, 81</i>(1), 140-150. https://doi.org/10.1021/acs.jnatprod.7b00780en_US
dc.identifier.cristinIDFRIDAID 1544143
dc.identifier.doi10.1021/acs.jnatprod.7b00780
dc.identifier.issn0163-3864
dc.identifier.issn1520-6025
dc.identifier.urihttps://hdl.handle.net/10037/14468
dc.language.isoengen_US
dc.publisherAmerican Chemical Societyen_US
dc.relation.journalJournal of natural products
dc.relation.projectIDinfo:eu-repo/grantAgreement/RCN/HAVKYST/184688/Norway/5 - Antibiotics from the sea - isolation and characterization of novel compounds from cold-water benthic organisms//en_US
dc.relation.projectIDinfo:eu-repo/grantAgreement/RCN/BIOTEK20201/208546/Norway/eXploring the BIOactive PEPtide Space of arctic marine invertebrates//en_US
dc.rights.accessRightsopenAccessen_US
dc.subjectVDP::Mathematics and natural science: 400::Chemistry: 440en_US
dc.subjectVDP::Matematikk og Naturvitenskap: 400::Kjemi: 440en_US
dc.titleParalithocins, Antimicrobial Peptides with Unusual Disulfide Connectivity from the Red King Crab, Paralithodes camtschaticusen_US
dc.typeJournal articleen_US
dc.typeTidsskriftartikkelen_US
dc.typePreprinten_US
dc.typeManuskripten_US


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