Issue 25, 2013
From the journal:

Organic & Biomolecular Chemistry

Chemoselective fragment condensation between peptide and peptidomimetic oligomers†

Paul M. Levine,a   Timothy W. Craven,b   Richard Bonneaubc  and  Kent Kirshenbaum*a  

* Corresponding authors

a Department of Chemistry, New York University, New York, New York, USA
E-mail: kent@nyu.edu
Tel: +1 212-998-8486

b Center for Genomics and Systems Biology, New York University, New York, New York, USA

c Courant Institute of Mathematical Sciences, Computer Science Department, New York University, New York, New York, USA

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.

Graphical abstract: Chemoselective fragment condensation between peptide and peptidomimetic oligomers

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Article information

DOI
https://doi.org/10.1039/C3OB40606G
Article type
Communication
Submitted
26 Mar 2013
Accepted
07 May 2013
First published
29 May 2013

Org. Biomol. Chem., 2013,11, 4142-4146

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Chemoselective fragment condensation between peptide and peptidomimetic oligomers

P. M. Levine, T. W. Craven, R. Bonneau and K. Kirshenbaum, Org. Biomol. Chem., 2013, 11, 4142 DOI: 10.1039/C3OB40606G

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