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Abstract
Stapling of peptides renders them ideal drug candidates. The individual characteristics of synthetic staple moities impact directly on the peptide’s final properties. We report a bioinspired ketenamine-based peptide staple resembling the natural metabolite lanthionine ketenamine. The strategy is orthogonal to most canonical amino acids, proceeds in water and allows for tailored linkers.
Supplementary materials
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Supporting Information
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Detailed experimental procedures and data, supplementary figures, schemes and tables.
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