Efficient chemoenzymatic synthesis of biotinylated human serum albumin-sialoglycoside conjugates containing O-acetylated sialic acids.
Sialyl Tn (STn) and sialyl lactoside derivatives containing O-acetylated sialic acid residues have been chemoenzymatically synthesized using a one-pot three-enzyme system and conjugated to biotinylated human serum albumin (HSA) using an adipic acid para-nitrophenyl ester coupling reagent. This approach provides an efficient and general protocol for preparing carbohydrate-protein conjugates containing base-sensitive groups.
Yu
Hai
H
Department of Chemistry, University of California-Davis, One Shields Avenue, Davis, CA 95616, USA.
Chokhawala
Harshal A
HA
Varki
Ajit
A
Chen
Xi
X
D000107:Acetylation; D001710:Biotin / Q000737:chemistry*; D006027:Glycosides / Q000737:chemistry*; D006801:Humans; D015394:Molecular Structure; D012709:Serum Albumin / Q000737:chemistry* / Q000378:metabolism*; D012794:Sialic Acids / Q000138:chemical synthesis* / Q000737:chemistry / Q000378:metabolism*; D012799:Sialyltransferases / Q000378:metabolism*; D019032:Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization
D006027:Glycosides; D012709:Serum Albumin; D012794:Sialic Acids; D001710:Biotin; D012799:Sialyltransferases