Intrinsic bioconjugation for site-specific protein PEGylation at N-terminal serine.
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).
Department of Chemistry, New York University, New York, 10003, USA. kent@nyu.edu.
Paul M
PM
Levine
Timothy W
TW
Craven
Richard
R
Bonneau
Kent
K
Kirshenbaum
D000447:Aldehydes / Q000737:chemistry*; D006801:Humans; D015394:Molecular Structure; D010446:Peptide Fragments / Q000737:chemistry*; D011092:Polyethylene Glycols / Q000737:chemistry*; D011487:Protein Conformation; D012260:Ribonucleases / Q000737:chemistry*; D012694:Serine / Q000737:chemistry*; D019032:Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization; D019379:Teriparatide / Q000031:analogs & derivatives* / Q000737:chemistry
D000447:Aldehydes; D010446:Peptide Fragments; D019379:Teriparatide; C013243:salicylaldehyde; D011092:Polyethylene Glycols; D012694:Serine; D012260:Ribonucleases; C022542:ribonuclease S; C035748:parathyroid hormone (1-34)amide