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Title: Functionalised staple linkages for modulating the cellular activity of stapled peptides
Authors: Lau, 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.
Issue Date: May-2014
Citation: Lau, 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.
Abstract: Stapled 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.
Source Title: Chemical Science
ISSN: 20416520
DOI: 10.1039/c4sc00045e
Appears in Collections:Staff Publications

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