Please use this identifier to cite or link to this item: https://doi.org/10.1039/c4sc00045e
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dc.titleFunctionalised staple linkages for modulating the cellular activity of stapled peptides
dc.contributor.authorLau, Y.H.
dc.contributor.authorDe Andrade, P.
dc.contributor.authorQuah, S.-T.
dc.contributor.authorRossmann, M.
dc.contributor.authorLaraia, L.
dc.contributor.authorSköld, N.
dc.contributor.authorSum, T.J.
dc.contributor.authorRowling, P.J.E.
dc.contributor.authorJoseph, T.L.
dc.contributor.authorVerma, C.
dc.contributor.authorHyvönen, M.
dc.contributor.authorItzhaki, L.S.
dc.contributor.authorVenkitaraman, A.R.
dc.contributor.authorBrown, C.J.
dc.contributor.authorLane, D.P.
dc.contributor.authorSpring, D.R.
dc.date.accessioned2014-10-27T08:29:03Z
dc.date.available2014-10-27T08:29:03Z
dc.date.issued2014-05
dc.identifier.citationLau, Y.H., De Andrade, P., Quah, S.-T., Rossmann, M., Laraia, L., Sköld, N., Sum, T.J., Rowling, P.J.E., Joseph, T.L., Verma, C., Hyvönen, M., Itzhaki, L.S., Venkitaraman, A.R., Brown, C.J., Lane, D.P., Spring, D.R. (2014-05). Functionalised staple linkages for modulating the cellular activity of stapled peptides. Chemical Science 5 (5) : 1804-1809. ScholarBank@NUS Repository. https://doi.org/10.1039/c4sc00045e
dc.identifier.issn20416520
dc.identifier.urihttp://scholarbank.nus.edu.sg/handle/10635/100728
dc.description.abstractStapled peptides are a promising class of alpha-helix mimetic inhibitors for protein-protein interactions. We report the divergent synthesis of "functionalised" stapled peptides via an efficient two-component strategy. Starting from a single unprotected diazido peptide, dialkynyl staple linkers bearing different unprotected functional motifs are introduced to create different alpha-helical peptides in one step, functionalised on the staple linkage itself. Applying this concept to the p53/MDM2 interaction, we improve the cell permeability and p53 activating capability of an otherwise impermeable p53 stapled peptide by introducing cationic groups on the staple linkage, rather than modifying the peptide sequence. © 2014 the Partner Organisations.
dc.description.urihttp://libproxy1.nus.edu.sg/login?url=http://dx.doi.org/10.1039/c4sc00045e
dc.sourceScopus
dc.typeArticle
dc.contributor.departmentBIOLOGICAL SCIENCES
dc.description.doi10.1039/c4sc00045e
dc.description.sourcetitleChemical Science
dc.description.volume5
dc.description.issue5
dc.description.page1804-1809
dc.description.codenCSHCC
dc.identifier.isiut000334492700015
Appears in Collections:Staff Publications

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