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- W1997799199 abstract "In vivo synthesis of peptides by bacterial expression has developed into a reliable alternative to solid-phase peptide synthesis. A significant drawback of in vivo methods is the difficulty with which gene products can be modified post-translationally. Here, we present a method for the facile modification of peptides generated in bacterial hosts after cyanogen bromide cleavage at C-terminal methionines. Reaction of the resulting homoserine lactones with propargylamine allows efficient and selective modification with a wide variety of chemicals such as fluorescent dyes, biotin derivatives, polyprenyls, lipids, polysaccharides, or peptides. Attachment of the cell penetrating peptide octa-arginine (R8) to peptides derived from the proapoptotic tumor suppressor Bak BH3 led to efficient cellular uptake and subsequent cytochrome c release from mitochondria, culminating in induction of apoptosis similar to that observed with peptides linked to R8 via the peptide backbone. These results highlight the significant potential for use of such tools in live cells." @default.
- W1997799199 created "2016-06-24" @default.
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- W1997799199 date "2011-08-15" @default.
- W1997799199 modified "2023-09-23" @default.
- W1997799199 title "Chemical Synthesis of Cell-Permeable Apoptotic Peptides from <i>in Vivo</i> Produced Proteins" @default.
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- W1997799199 doi "https://doi.org/10.1021/bc200338u" @default.
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