Semisynthesis of peptoid-protein hybrids by chemical ligation at serine

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

Research output: Contribution to journalArticle

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 languageEnglish (US)
Pages (from-to)512-515
Number of pages4
JournalOrganic Letters
Volume16
Issue number2
DOIs
StatePublished - 2014

Fingerprint

Peptoids
Serine
Ligation
proteins
Bearings (structural)
Proteins
hormones
polypeptides
Parathyroid Hormone
Macromolecules
oligomers
Oligomers
macromolecules
esters
Hormones
Peptides
Therapeutics

ASJC Scopus subject areas

  • Organic Chemistry
  • Physical and Theoretical Chemistry
  • Biochemistry

Cite this

Semisynthesis of peptoid-protein hybrids by chemical ligation at serine. / Levine, Paul M.; Craven, Timothy W.; Bonneau, Richard; Kirshenbaum, Kent.

In: Organic Letters, Vol. 16, No. 2, 2014, p. 512-515.

Research output: Contribution to journalArticle

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