Dendritic sugar-microarrays by click chemistry

Tomohiro Fukuda; Shunsuke Onogi; Yoshiko Miura

doi:10.1016/j.tsf.2009.07.109

Dendritic sugar-microarrays by click chemistry

Tomohiro Fukuda, Shunsuke Onogi, Yoshiko Miura

Research output: Contribution to journal › Article › peer-review

41 Citations (Scopus)

Abstract

Saccharide microarrays with well-defined multivalency were prepared using glycodendrimers. The glycodendrimers with various generations and saccharides (α-Man, β-GlcNAc and β-Gal) were synthesized and immobilized on an acetylenyl-terminated gold substrate via click chemistry. The saccharide-immobilized substrates were analyzed using XPS, ellipsometry, cyclic voltammetry, contact angle goniometry, QCM and FTIR-RAS. The biological abilities of the saccharide-immobilized substrates were evaluated by SPR with the lectins of Con A, WGA and RCA₁₂₀. Lectin binding to the glycodendrimer array was quantitatively analyzed, and association constants (K_A) and kinetic rate constants (k_a and k_d) were evaluated. These kinetic constants were unique to each lectin, implying specificity of the multivalent effect of saccharide-lectin interaction.

Original language	English
Pages (from-to)	880-888
Number of pages	9
Journal	Thin Solid Films
Volume	518
Issue number	2
DOIs	https://doi.org/10.1016/j.tsf.2009.07.109
Publication status	Published - Nov 30 2009
Externally published	Yes

All Science Journal Classification (ASJC) codes

Electronic, Optical and Magnetic Materials
Surfaces and Interfaces
Surfaces, Coatings and Films
Metals and Alloys
Materials Chemistry

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10.1016/j.tsf.2009.07.109

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title = "Dendritic sugar-microarrays by click chemistry",

abstract = "Saccharide microarrays with well-defined multivalency were prepared using glycodendrimers. The glycodendrimers with various generations and saccharides (α-Man, β-GlcNAc and β-Gal) were synthesized and immobilized on an acetylenyl-terminated gold substrate via click chemistry. The saccharide-immobilized substrates were analyzed using XPS, ellipsometry, cyclic voltammetry, contact angle goniometry, QCM and FTIR-RAS. The biological abilities of the saccharide-immobilized substrates were evaluated by SPR with the lectins of Con A, WGA and RCA120. Lectin binding to the glycodendrimer array was quantitatively analyzed, and association constants (KA) and kinetic rate constants (ka and kd) were evaluated. These kinetic constants were unique to each lectin, implying specificity of the multivalent effect of saccharide-lectin interaction.",

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AU - Fukuda, Tomohiro

AU - Onogi, Shunsuke

AU - Miura, Yoshiko

PY - 2009/11/30

Y1 - 2009/11/30

N2 - Saccharide microarrays with well-defined multivalency were prepared using glycodendrimers. The glycodendrimers with various generations and saccharides (α-Man, β-GlcNAc and β-Gal) were synthesized and immobilized on an acetylenyl-terminated gold substrate via click chemistry. The saccharide-immobilized substrates were analyzed using XPS, ellipsometry, cyclic voltammetry, contact angle goniometry, QCM and FTIR-RAS. The biological abilities of the saccharide-immobilized substrates were evaluated by SPR with the lectins of Con A, WGA and RCA120. Lectin binding to the glycodendrimer array was quantitatively analyzed, and association constants (KA) and kinetic rate constants (ka and kd) were evaluated. These kinetic constants were unique to each lectin, implying specificity of the multivalent effect of saccharide-lectin interaction.

AB - Saccharide microarrays with well-defined multivalency were prepared using glycodendrimers. The glycodendrimers with various generations and saccharides (α-Man, β-GlcNAc and β-Gal) were synthesized and immobilized on an acetylenyl-terminated gold substrate via click chemistry. The saccharide-immobilized substrates were analyzed using XPS, ellipsometry, cyclic voltammetry, contact angle goniometry, QCM and FTIR-RAS. The biological abilities of the saccharide-immobilized substrates were evaluated by SPR with the lectins of Con A, WGA and RCA120. Lectin binding to the glycodendrimer array was quantitatively analyzed, and association constants (KA) and kinetic rate constants (ka and kd) were evaluated. These kinetic constants were unique to each lectin, implying specificity of the multivalent effect of saccharide-lectin interaction.

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Dendritic sugar-microarrays by click chemistry

Abstract

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