Controlled synthesis of glycopolymers with pendant complex-type sialylglycopeptides and their binding affinity with a lectin and an influenza virus
| Autor: | Tomonari Tanaka, Keiko Sakakibara, Keita Nakashima, Jianxin Zhao, Takashi Suzuki, Tadanobu Takahashi, Sotaro Tsuji, Xiaoyu Han, Yoshitomo Honda, Yuuki Kurebayashi |
|---|---|
| Rok vydání: | 2019 |
| Předmět: |
chemistry.chemical_classification
Acrylate Polymers and Plastics biology Chemistry Stereochemistry Organic Chemistry Lectin Sambucus sieboldiana Bioengineering 02 engineering and technology Oligosaccharide 010402 general chemistry 021001 nanoscience & nanotechnology biology.organism_classification 01 natural sciences Biochemistry 0104 chemical sciences chemistry.chemical_compound Agglutinin Polymerization biology.protein Copolymer 0210 nano-technology Cytotoxicity |
| Zdroj: | Polymer Chemistry. 10:5124-5130 |
| ISSN: | 1759-9962 1759-9954 |
| DOI: | 10.1039/c9py00745h |
| Popis: | Glycopolymers bearing complex-type sialylglycopeptides (SGPs) were synthesized using polymers with pendant-activated esters, poly(N-succinimidyl acrylate)s (polyNSAs), and SGP in which N-acetylneuraminic acids were presented at the nonreducing ends. The SGP-grafted copolymers were synthesized successfully by post-polymerization modification of an amino group of SGP with N-succinimidyl esters on the polyNSAs, with different degrees of polymerization (DPs) and degrees of substitution (DSs) of SGP. The resulting glycopolymers bearing SGPs exhibited strong interaction with the corresponding lectin Sambucus sieboldiana agglutinin with higher association constant (Ka) values of the order of 107 M−1. Moreover, the glycopolymers bearing SGPs interacted strongly with the human influenza A virus because of the multivalency of the oligosaccharide moieties on the polymer backbone. Their binding affinities increased with increasing DP and DS of SGP. The glycopolymers did not potentially induce cytotoxicity in the cells. |
| Databáze: | OpenAIRE |
| Externí odkaz: |
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