Cyanogen bromide cleavage generates fragments suitable for expressed protein and glycoprotein ligation.
Herein cyanogen bromide is employed for the efficient production of N-terminal cysteine containing protein fragments for expressed protein ligation (EPL) from polyhistidine-tagged precursors. We provide three examples of efficient CNBr cleavage of fragments of the glycoprotein erythropoietin that can be ligated with peptides or glycopeptide mimetics potentially giving rise to semisynthetic glycoprotein therapeutics.
School of Chemistry, University of Edinburgh, Kings Buildings, West Mains Road, Edinburgh, Scotland, UK. derek.macmillan@ed.ac.uk
Derek
D
Macmillan
Lubna
L
Arham
D002846:Chromatography, Affinity; D003488:Cyanogen Bromide / Q000737:chemistry*; D003545:Cysteine / Q000737:chemistry; D004921:Erythropoietin / Q000138:chemical synthesis / Q000737:chemistry; D006023:Glycoproteins / Q000138:chemical synthesis*; D006639:Histidine / Q000737:chemistry; D010446:Peptide Fragments / Q000737:chemistry*; D015202:Protein Engineering / Q000379:methods; D011506:Proteins / Q000138:chemical synthesis*
D006023:Glycoproteins; D010446:Peptide Fragments; D011506:Proteins; D004921:Erythropoietin; C033223:polyhistidine; D006639:Histidine; D003545:Cysteine; D003488:Cyanogen Bromide