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Aqueous synthesis of sialylglycopeptide‐grafted glycopolymers with high affinity for the lectin and the influenza virus hemagglutinin
Author(s) -
Tsuji Sotaro,
Aso Yuji,
Ohara Hitomi,
Tanaka Tomonari
Publication year - 2020
Publication title -
journal of polymer science
Language(s) - English
Resource type - Journals
eISSN - 2642-4169
pISSN - 2642-4150
DOI - 10.1002/pol.20190184
Subject(s) - chemistry , lectin , residue (chemistry) , aqueous solution , hemagglutinin (influenza) , polymer chemistry , lysine , quartz crystal microbalance , glycan , amino acid , organic chemistry , biochemistry , adsorption , glycoprotein , gene
Glycopolymers with pendant complex‐type sialyl N ‐glycans containing heptapeptides, that is, sialylglycopeptides (SGPs), were synthesized using a water soluble polymer backbone bearing N ‐hydroxysulfosuccinimidyl esters by post‐polymerization modification in water. Although SGP has three amino groups on the peptide chain, the substitution reaction occurs preferentially at the N ‐terminus α‐amino group in the lysine residue onto the polymer side chain because the reactivity of such α‐amino group is higher than that of the ε‐amino group in the lysine residue under mild acidic aqueous condition. The resulting SGP‐grafted glycopolymers exhibited strong interaction with the lectin Sambucus sieboldiana agglutinin and the human influenza A virus hemagglutinin, with higher binding associate constant values than those of free saccharide according to quartz crystal microbalance analysis. © 2020 Wiley Periodicals, Inc. J. Polym. Sci. 2020 , 58 , 548–556