Total Synthesis of the Spider-Venom Peptide Hi1a

dc.contributor.authorDuggan, N.M.
dc.contributor.authorSaez, N.J.
dc.contributor.authorClayton, D.
dc.contributor.authorBudusan, E.
dc.contributor.authorWatson, E.E.
dc.contributor.authorTucker, I.J.
dc.contributor.authorRash, L.D.
dc.contributor.authorKing, G.F.
dc.contributor.authorPayne, R.J.
dc.date.issued2021
dc.description.abstractHi1a is a venom peptide from the Australian funnelweb spider Hadronyche infensa with a complex tertiary structure. Hi1a has neuroprotective and cardioprotective properties due to its potent inhibition of acid-sensing ion channel 1a (ASIC1a) and is currently being pursued as a novel therapy for acute ischemic events. Herein, we describe the total synthesis of Hi1a using native chemical ligation. The synthetic peptide was successfully folded and exhibited similar inhibitory activity on ASIC1a to recombinant Hi1a.
dc.description.statementofresponsibilityNisharnthi M. Duggan, Natalie J. Saez, Daniel Clayton, Elena Budusan, Emma E. Watson, Isaac J. Tucker, Lachlan D. Rash, Glenn F. King, and Richard J. Payne
dc.identifier.citationOrganic Letters, 2021; 23(21):8375-8379
dc.identifier.doi10.1021/acs.orglett.1c03112
dc.identifier.issn1523-7060
dc.identifier.issn1523-7052
dc.identifier.orcidWatson, E.E. [0000-0001-5946-473X]
dc.identifier.urihttps://hdl.handle.net/2440/136100
dc.language.isoen
dc.publisherAmerican Chemical Society
dc.relation.granthttp://purl.org/au-research/grants/arc/CE200100012
dc.relation.granthttp://purl.org/au-research/grants/nhmrc/1154622
dc.relation.granthttp://purl.org/au-research/grants/nhmrc/1136889
dc.rights© 2021 American Chemical Society
dc.source.urihttps://doi.org/10.1021/acs.orglett.1c03112
dc.subjectAnimals
dc.subjectSpiders
dc.subjectPeptides
dc.subjectSpider Venoms
dc.subjectMolecular Structure
dc.subjectAcid Sensing Ion Channels
dc.subject.meshSpider Venoms
dc.titleTotal Synthesis of the Spider-Venom Peptide Hi1a
dc.typeJournal article
pubs.publication-statusPublished

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