A bimane‐based peptide staple for combined helical induction and fluorescent imaging

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dc.contributor.authorHorsfall, A.J.
dc.contributor.authorDunning, K.R.
dc.contributor.authorKeeling, K.L.
dc.contributor.authorScanlon, D.B.
dc.contributor.authorWegener, K.L.
dc.contributor.authorAbell, A.D.
dc.date.issued2020
dc.description.abstractThe thiol-selective fluorescent imaging agent, dibromobimane, has been repurposed to crosslink cysteine- and homocysteine- containing peptides, with the resulting bimane linker acting as both a structural constraint and a fluorescent tag. Macro- cyclisation was conducted on nine short peptides containing two cysteines and/or homocysteines, both on-resin and in buffered aqueous solution, to give macrocycles ranging in size from 16 (i,i +2) to 31 (i,i + 7) atoms. The structures were defined by CD, NMR structure calculations by using Xplor-NIH, NMR secondary shift and J HαNH analyses to reveal helical structure in the i,i + 4 (1, 2), and i,i + 3 (5) constrained peptides. Cellular- uptake studies were conducted with three of the macrocycles. Subsequent confocal imaging revealed punctate fluorescence within the cytosol indicative of peptides trapped in endocytic vesicles. These studies demonstrate that dibromobimane is an effective tool for defining secondary structure within short peptides, whilst simultaneously introducing a fluorescent tag suitable for common cell-based experiments.
dc.description.statementofresponsibilityAimee J. Horsfall, Kylie R. Dunning, Kelly L. Keeling, Denis B. Scanlon, Kate L. Wegener, Andrew D. Abell
dc.identifier.citationChemBioChem, 2020; 21(23):1-11
dc.identifier.doi10.1002/cbic.202000485
dc.identifier.issn1439-7633
dc.identifier.issn1439-7633
dc.identifier.orcidHorsfall, A.J. [0000-0003-1276-2742]
dc.identifier.orcidDunning, K.R. [0000-0002-0462-6479]
dc.identifier.orcidWegener, K.L. [0000-0002-1562-6060]
dc.identifier.orcidAbell, A.D. [0000-0002-0604-2629]
dc.identifier.urihttp://hdl.handle.net/2440/127446
dc.language.isoen
dc.publisherWiley
dc.relation.granthttp://purl.org/au-research/grants/arc/CE140100003
dc.rights© 2020 Wiley‐VCH GmbH
dc.source.urihttps://doi.org/10.1002/cbic.202000485
dc.subjectBimane; fluorescence; helical structures; peptide staple; peptidomimetics
dc.titleA bimane‐based peptide staple for combined helical induction and fluorescent imaging
dc.typeJournal article
pubs.publication-statusPublished

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