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

Chem Commun (Camb). 2014 Jul 4;50(52):6909-12. doi: 10.1039/c4cc01928h.

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).

Publication types

  • Research Support, N.I.H., Extramural
  • Research Support, Non-U.S. Gov't
  • Research Support, U.S. Gov't, Non-P.H.S.

MeSH terms

  • Aldehydes / chemistry*
  • Humans
  • Molecular Structure
  • Peptide Fragments / chemistry*
  • Polyethylene Glycols / chemistry*
  • Protein Conformation
  • Ribonucleases / chemistry*
  • Serine / chemistry*
  • Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization
  • Teriparatide / analogs & derivatives*
  • Teriparatide / chemistry

Substances

  • Aldehydes
  • Peptide Fragments
  • Teriparatide
  • salicylaldehyde
  • Polyethylene Glycols
  • Serine
  • Ribonucleases
  • ribonuclease S
  • parathyroid hormone (1-34)amide