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dc.contributor.authorHansen, Ida Kristine Østnes
dc.contributor.authorLövdahl, Tomas
dc.contributor.authorSimonovic, Danijela
dc.contributor.authorØstnes Hansen, Kine
dc.contributor.authorAndersen, Aaron John Christian
dc.contributor.authorDevold, hege
dc.contributor.authorRichard, Céline Sarah Marine
dc.contributor.authorAndersen, Jeanette Hammer
dc.contributor.authorStrøm, Morten B.
dc.contributor.authorHaug, Tor
dc.date.accessioned2020-08-25T11:19:04Z
dc.date.available2020-08-25T11:19:04Z
dc.date.issued2020-07-30
dc.description.abstractTurgencin A, a potent antimicrobial peptide isolated from the Arctic sea squirt <i>Synoicum turgens</i>, consists of 36 amino acid residues and three disulfide bridges, making it challenging to synthesize. The aim of the present study was to develop a truncated peptide with an antimicrobial drug lead potential based on turgencin A. The experiments consisted of: (1) sequence analysis and prediction of antimicrobial potential of truncated 10-mer sequences; (2) synthesis and antimicrobial screening of a lead peptide devoid of the cysteine residues; (3) optimization of in vitro antimicrobial activity of the lead peptide using an amino acid replacement strategy; and (4) screening the synthesized peptides for cytotoxic activities. In silico analysis of turgencin A using various prediction software indicated an internal, cationic 10-mer sequence to be putatively antimicrobial. The synthesized truncated lead peptide displayed weak antimicrobial activity. However, by following a systematic amino acid replacement strategy, a modified peptide was developed that retained the potency of the original peptide. The optimized peptide <b>StAMP-9</b> displayed bactericidal activity, with minimal inhibitory concentrations of 7.8 µg/mL against <i>Staphylococcus aureus</i> and 3.9 µg/mL against <i>Escherichia coli</i>, and no cytotoxic effects against mammalian cells. Preliminary experiments indicate the bacterial membranes as immediate and primary targets.en_US
dc.identifier.citationHansen IK, Lövdahl, Simonovic D, Østnes Hansen KØH, Andersen AJC, Devold h, Richard CSM, Andersen JH, Strøm mbs, Haug T. Antimicrobial activity of small synthetic peptides based on the marine peptide turgencin A: Prediction of antimicrobial peptide sequences in a natural peptide and strategy for optimization of potency. International Journal of Molecular Sciences. 2020;21(15)
dc.identifier.cristinIDFRIDAID 1824308
dc.identifier.doihttps://doi.org/10.3390/ijms21155460
dc.identifier.issn1422-0067
dc.identifier.urihttps://hdl.handle.net/10037/19147
dc.language.isoengen_US
dc.publisherMDPIen_US
dc.relation.ispartofHansen, I.K.Ø. (2022). Antimicrobial peptides from the Arctic ascidian <i>Synoicum turgens</i>. (Doctoral thesis). <a href=https://hdl.handle.net/10037/25305>https://hdl.handle.net/10037/25305</a>.
dc.relation.journalInternational Journal of Molecular Sciences
dc.rights.holderCopyright 2020 The Author(s)en_US
dc.subjectVDP::Agriculture and fishery disciplines: 900::Fisheries science: 920en_US
dc.subjectVDP::Landbruks- og Fiskerifag: 900::Fiskerifag: 920en_US
dc.titleAntimicrobial activity of small synthetic peptides based on the marine peptide turgencin A: Prediction of antimicrobial peptide sequences in a natural peptide and strategy for optimization of potencyen_US
dc.type.versionpublishedVersionen_US
dc.typeJournal articleen_US
dc.typeTidsskriftartikkelen_US
dc.typePeer revieweden_US


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