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

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

Research output: Contribution to journalArticle

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).

Original languageEnglish (US)
Pages (from-to)6909-6912
Number of pages4
JournalChemical Communications
Volume50
Issue number52
DOIs
StatePublished - Jul 4 2014

Fingerprint

Serine
Ligation
Proteins
Polypeptides
Parathyroid Hormone
Polyethylene glycols
Esters
Peptides
Therapeutics
salicylaldehyde
ribonuclease S
Ribonucleases

ASJC Scopus subject areas

  • Chemistry(all)
  • Catalysis
  • Ceramics and Composites
  • Electronic, Optical and Magnetic Materials
  • Surfaces, Coatings and Films
  • Materials Chemistry
  • Metals and Alloys
  • Medicine(all)

Cite this

Intrinsic bioconjugation for site-specific protein PEGylation at N-terminal serine. / Levine, Paul M.; Craven, Timothy W.; Bonneau, Richard; Kirshenbaum, Kent.

In: Chemical Communications, Vol. 50, No. 52, 04.07.2014, p. 6909-6912.

Research output: Contribution to journalArticle

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