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dc.contributor.authorLogashina, Yulia A.
dc.contributor.authorSolstad, Runar Gjerp
dc.contributor.authorMineev, Konstantin S.
dc.contributor.authorKorolkova, Yuliya V.
dc.contributor.authorMosharova, Irina V.
dc.contributor.authorDyachenko, Igor A.
dc.contributor.authorPalikov, Victor A.
dc.contributor.authorPalikova, Yulia A.
dc.contributor.authorMurashev, Arkadii N.
dc.contributor.authorArseniev, Alexander S.
dc.contributor.authorKozlov, Sergey A.
dc.contributor.authorStensvåg, Klara
dc.contributor.authorHaug, Tor
dc.contributor.authorAndreev, Yaroslav A.
dc.date.accessioned2018-03-20T12:26:52Z
dc.date.available2018-03-20T12:26:52Z
dc.date.issued2017-04-29
dc.description.abstractA novel bioactive peptide named τ-AnmTx Ueq 12-1 (short name Ueq 12-1) was isolated and characterized from the sea anemone Urticina eques. Ueq 12-1 is unique among the variety of known sea anemone peptides in terms of its primary and spatial structure. It consists of 45 amino acids including 10 cysteine residues with an unusual distribution and represents a new group of sea anemone peptides. The 3D structure of Ueq 12-1, determined by NMR spectroscopy, represents a new disulfide-stabilized fold partly similar to the defensin-like fold. Ueq 12-1 showed the dual activity of both a moderate antibacterial activity against Gram-positive bacteria and a potentiating activity on the transient receptor potential ankyrin 1 (TRPA1). Ueq 12-1 is a unique peptide potentiator of the TRPA1 receptor that produces analgesic and anti-inflammatory effects in vivo. The antinociceptive properties allow us to consider Ueq 12-1 as a potential analgesic drug lead with antibacterial properties.en_US
dc.description.sponsorshipPresidium of RAS “Molecular and Cell Biology” from the President of RF Russian Science Foundationen_US
dc.descriptionSource at <a href=https://doi.org/10.3390/toxins9050154> https://doi.org/10.3390/toxins9050154 </a>.en_US
dc.identifier.citationLogashina, Y.A., Solstad, R.G., Mineev, K.S., Korolkova, Y.V., Mosharova, I.V., Dyachenko, I.A. ... Andreev, Y.A. (2017). New Disulfide-Stabilized Fold Provides Sea Anemone Peptide to Exhibit Both Antimicrobial and TRPA1 Potentiating Properties. Toxins, 9(5).en_US
dc.identifier.cristinIDFRIDAID 1467584
dc.identifier.doi10.3390/toxins9050154
dc.identifier.issn2072-6651
dc.identifier.urihttps://hdl.handle.net/10037/12386
dc.language.isoengen_US
dc.publisherMDPIen_US
dc.relation.journalToxins
dc.relation.projectIDNorges forskningsråd: 208546en_US
dc.relation.projectIDinfo:eu-repo/grantAgreement/RCN/BIOTEK2021/208546/Norway/eXploring the BIOactive PEPtide Space of arctic marine invertebrates//en_US
dc.rights.accessRightsopenAccessen_US
dc.subjectsea anemonesen_US
dc.subjectinnate immunityen_US
dc.subjectdefensive strategiesen_US
dc.subjectTRPA1 receptoren_US
dc.subjectantimicrobialen_US
dc.subjectVDP::Matematikk og Naturvitenskap: 400::Zoologiske og botaniske fag: 480::Marinbiologi: 497en_US
dc.subjectVDP::Mathematics and natural science: 400::Zoology and botany: 480::Marine biology: 497en_US
dc.titleNew Disulfide-Stabilized Fold Provides Sea Anemone Peptide to Exhibit Both Antimicrobial and TRPA1 Potentiating Propertiesen_US
dc.typeJournal articleen_US
dc.typeTidsskriftartikkelen_US
dc.typePeer revieweden_US


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