Chemoselective fragment condensation between peptide and peptidomimetic oligomers

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

Research output: Contribution to journalArticle

Abstract

We report the first example of chemoselective fragment condensation, through native amide bond formation, between peptoid and peptide oligomers. Peptoid oligomers bearing C-terminal salicylaldehyde esters were synthesized and ligated to peptides containing N-terminal serine or threonine residues. We investigate the ligation efficiency of peptoid oligomers varying in length, sequence, and C-terminal steric bulk. These protocols enhance accessibility of structurally complex peptoid-peptide hybrids and will facilitate the design new semi-synthetic proteins with unique attributes.

Original languageEnglish (US)
Pages (from-to)4142-4146
Number of pages5
JournalOrganic and Biomolecular Chemistry
Volume11
Issue number25
DOIs
StatePublished - Jul 7 2013

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Peptoids
Peptidomimetics
oligomers
Oligomers
peptides
Condensation
condensation
fragments
Peptides
Bearings (structural)
amides
esters
Threonine
Amides
Serine
proteins
Ligation
Proteins

ASJC Scopus subject areas

  • Physical and Theoretical Chemistry
  • Organic Chemistry
  • Biochemistry

Cite this

Chemoselective fragment condensation between peptide and peptidomimetic oligomers. / Levine, Paul M.; Craven, Timothy W.; Bonneau, Richard; Kirshenbaum, Kent.

In: Organic and Biomolecular Chemistry, Vol. 11, No. 25, 07.07.2013, p. 4142-4146.

Research output: Contribution to journalArticle

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