Issue 52, 2014
From the journal:

Chemical Communications

Intrinsic bioconjugation for site-specific protein PEGylation at N-terminal serine†

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, USA
E-mail: kent@nyu.edu

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

c Courant Institute of Mathematical Sciences, New York University, New York, USA

Abstract

Recently developed chemical ligation protocols were elaborated for rapid N-terminal protein PEGylation. We introduce a PEG-salicylaldehyde ester and demonstrate its site-specific ligation to the N-terminus of the RNase S protein and to the therapeutic polypeptide PTH (1–34).

Graphical abstract: Intrinsic bioconjugation for site-specific protein PEGylation at N-terminal serine

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Article information

DOI
https://doi.org/10.1039/C4CC01928H
Article type
Communication
Submitted
14 Mar 2014
Accepted
29 Apr 2014
First published
19 May 2014

Chem. Commun., 2014,50, 6909-6912

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Intrinsic bioconjugation for site-specific protein PEGylation at N-terminal serine

P. M. Levine, T. W. Craven, R. Bonneau and K. Kirshenbaum, Chem. Commun., 2014, 50, 6909 DOI: 10.1039/C4CC01928H

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