Semisynthesis of peptoid-protein hybrids by chemical ligation at serine

Paul M. Levine; Timothy W. Craven; Richard Bonneau; Kent Kirshenbaum

doi:10.1021/ol4033978

Semisynthesis of peptoid-protein hybrids by chemical ligation at serine

Paul M. Levine, Timothy W. Craven, Richard Bonneau, Kent Kirshenbaum

Research output: Contribution to journal › Article › peer-review

Abstract

Chemical ligation protocols were explored for generating semisynthetic peptoid-protein hybrid architectures containing a native serine residue at the ligation site. Peptoid oligomers bearing C-terminal salicylaldehyde esters were synthesized and ligated to the N-terminus of the RNase S protein or the therapeutic hormone PTH(1-34) polypeptide. This technique will expand the repertoire of strategies to enable design of hybrid macromolecules with novel structures and functions not accessible to fully biosynthesized proteins.

Original language	English (US)
Pages (from-to)	512-515
Number of pages	4
Journal	Organic Letters
Volume	16
Issue number	2
DOIs	https://doi.org/10.1021/ol4033978
State	Published - Jan 17 2014

ASJC Scopus subject areas

Biochemistry
Physical and Theoretical Chemistry
Organic Chemistry

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10.1021/ol4033978

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abstract = "Chemical ligation protocols were explored for generating semisynthetic peptoid-protein hybrid architectures containing a native serine residue at the ligation site. Peptoid oligomers bearing C-terminal salicylaldehyde esters were synthesized and ligated to the N-terminus of the RNase S protein or the therapeutic hormone PTH(1-34) polypeptide. This technique will expand the repertoire of strategies to enable design of hybrid macromolecules with novel structures and functions not accessible to fully biosynthesized proteins.",

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AU - Craven, Timothy W.

AU - Bonneau, Richard

AU - Kirshenbaum, Kent

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AB - Chemical ligation protocols were explored for generating semisynthetic peptoid-protein hybrid architectures containing a native serine residue at the ligation site. Peptoid oligomers bearing C-terminal salicylaldehyde esters were synthesized and ligated to the N-terminus of the RNase S protein or the therapeutic hormone PTH(1-34) polypeptide. This technique will expand the repertoire of strategies to enable design of hybrid macromolecules with novel structures and functions not accessible to fully biosynthesized proteins.

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Semisynthesis of peptoid-protein hybrids by chemical ligation at serine

Abstract

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