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dc.contributor.authorDey, Hymonti
dc.contributor.authorSimonovic, Danijela
dc.contributor.authorHagen, Ingrid Sofie Norberg-Schulz
dc.contributor.authorVasskog, Terje
dc.contributor.authorFredheim, Elizabeth G. Aarag
dc.contributor.authorBlencke, Hans-Matti
dc.contributor.authorAnderssen, Trude
dc.contributor.authorStrøm, Morten B.
dc.contributor.authorHaug, Tor
dc.date.accessioned2022-11-18T11:52:54Z
dc.date.available2022-11-18T11:52:54Z
dc.date.issued2022-11-10
dc.description.abstractWe have synthesised short analogues of the marine antimicrobial peptide Turgencin A from the colonial Arctic ascidian Synoicum turgens. In this study, we focused on a central, cationic 12-residue Cys-Cys loop region within the sequence. Modified (tryptophan- and arginine-enriched) linear peptides were compared with Cys-Cys cyclic derivatives, and both linear and Cys-cyclic peptides were N-terminally acylated with octanoic acid (C<sub>8</sub> ), decanoic acid (C<sub>10</sub>) or dodecanoic acid (C<sub>12</sub>). The highest antimicrobial potency was achieved by introducing dodecanoic acid to a cyclic Turgencin A analogue with low intrinsic hydrophobicity, and by introducing octanoic acid to a cyclic analogue displaying a higher intrinsic hydrophobicity. Among all tested synthetic Turgencin A lipopeptide analogues, the most promising candidates regarding both antimicrobial and haemolytic activity were C<sub>12</sub>-cTurg-1 and C<sub>8</sub>-cTurg-2. These optimized cyclic lipopeptides displayed minimum inhibitory concentrations of 4 µg/mL against Staphylococcus aureus, Escherichia coli and the fungus Rhodothorula sp. Mode of action studies on bacteria showed a rapid membrane disruption and bactericidal effect of the cyclic lipopeptides. Haemolytic activity against human erythrocytes was low, indicating favorable selective targeting of bacterial cells.en_US
dc.identifier.citationDey H, Simonovic D, Hagen IN, Vasskog TV, Fredheim E, Blencke H, Anderssen T, Strøm mbs, Haug T. Synthesis and Antimicrobial Activity of Short Analogues of the Marine Antimicrobial Peptide Turgencin A: Effects of SAR Optimizations, Cys-Cys Cyclization and Lipopeptide Modifications. International Journal of Molecular Sciences. 2022;23(22)en_US
dc.identifier.cristinIDFRIDAID 2072594
dc.identifier.doi10.3390/ijms232213844
dc.identifier.issn1661-6596
dc.identifier.issn1422-0067
dc.identifier.urihttps://hdl.handle.net/10037/27420
dc.language.isoengen_US
dc.publisherMDPIen_US
dc.relation.ispartofSimonovic, D. (2023). Synthesis and structure-activity relationship studies of marine-derived antimicrobial peptides and small cyclic peptidomimetics. (Doctoral thesis). <a href=https://hdl.handle.net/10037/29375>https://hdl.handle.net/10037/29375</a>.
dc.relation.ispartofDey, H. (2024). Antimicrobial activities and mechanisms of action of peptide analogues of marine origin. (Doctoral thesis). <a href=https://hdl.handle.net/10037/33605>https://hdl.handle.net/10037/33605</a>
dc.relation.journalInternational Journal of Molecular Sciences
dc.rights.accessRightsopenAccessen_US
dc.rights.holderCopyright 2022 The Author(s)en_US
dc.rights.urihttps://creativecommons.org/licenses/by/4.0en_US
dc.rightsAttribution 4.0 International (CC BY 4.0)en_US
dc.subjectVDP::Matematikk og naturvitenskap: 400::Kjemi: 440::Legemiddelkjemi: 448en_US
dc.subjectVDP::Mathematics and natural scienses: 400::Chemistry: 440::Pharmaceutical chemistry: 448en_US
dc.subjectMikrobiologi / Microbiologyen_US
dc.titleSynthesis and Antimicrobial Activity of Short Analogues of the Marine Antimicrobial Peptide Turgencin A: Effects of SAR Optimizations, Cys-Cys Cyclization and Lipopeptide Modificationsen_US
dc.type.versionpublishedVersionen_US
dc.typeJournal articleen_US
dc.typeTidsskriftartikkelen_US
dc.typePeer revieweden_US


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Attribution 4.0 International (CC BY 4.0)
Med mindre det står noe annet, er denne innførselens lisens beskrevet som Attribution 4.0 International (CC BY 4.0)