Sugar microarray via click chemistry: molecular recognition with lectins and amyloid β (1–42)

Sugar microarrays were fabricated on various substrates via click chemistry. Acetylene-terminated substrates were prepared by forming self-assembled monolayers (SAMs) on a gold substrate with alkyl-disulfide and on silicon, quartz and glass substrates with a silane-coupling reagent. The gold substra...

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Main Author: Erino Matsumoto, Takahiro Yamauchi, Tomohiro Fukuda and Yoshiko Miura
Format: Article
Language:English
Published: Taylor & Francis Group 2009-01-01
Series:Science and Technology of Advanced Materials
Subjects:
Online Access:http://www.iop.org/EJ/abstract/1468-6996/10/3/034605
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spelling doaj-3e3961bb9bdd4566ac0291a0c85741852020-11-25T01:07:35ZengTaylor & Francis GroupScience and Technology of Advanced Materials1468-69961878-55142009-01-01103034605Sugar microarray via click chemistry: molecular recognition with lectins and amyloid β (1–42)Erino Matsumoto, Takahiro Yamauchi, Tomohiro Fukuda and Yoshiko MiuraSugar microarrays were fabricated on various substrates via click chemistry. Acetylene-terminated substrates were prepared by forming self-assembled monolayers (SAMs) on a gold substrate with alkyl-disulfide and on silicon, quartz and glass substrates with a silane-coupling reagent. The gold substrates were subjected to surface plasmon resonance measurements, and the quartz and glass substrates were subjected to spectroscopy measurements and optical microscopy observation. The saccharide-immobilized substrate on the gold substrate showed specific interaction with the corresponding lectin, and the saccharides showed inert surface properties to other proteins with a high signal-to-noise ratio. We also focused on the saccharide–protein interaction on protein amyloidosis of Alzheimer amyloid β. Amyloid β peptide showed conformation transition on the saccharide-immobilization substrate into a β-sheet, and fibril formation and amyloid aggregates were found on the specific saccharides.http://www.iop.org/EJ/abstract/1468-6996/10/3/034605self-assembled monolayersaccharidemicroarraysurface plasmon resonanceamyloidAlzheimer
collection DOAJ
language English
format Article
sources DOAJ
author Erino Matsumoto, Takahiro Yamauchi, Tomohiro Fukuda and Yoshiko Miura
spellingShingle Erino Matsumoto, Takahiro Yamauchi, Tomohiro Fukuda and Yoshiko Miura
Sugar microarray via click chemistry: molecular recognition with lectins and amyloid β (1–42)
Science and Technology of Advanced Materials
self-assembled monolayer
saccharide
microarray
surface plasmon resonance
amyloid
Alzheimer
author_facet Erino Matsumoto, Takahiro Yamauchi, Tomohiro Fukuda and Yoshiko Miura
author_sort Erino Matsumoto, Takahiro Yamauchi, Tomohiro Fukuda and Yoshiko Miura
title Sugar microarray via click chemistry: molecular recognition with lectins and amyloid β (1–42)
title_short Sugar microarray via click chemistry: molecular recognition with lectins and amyloid β (1–42)
title_full Sugar microarray via click chemistry: molecular recognition with lectins and amyloid β (1–42)
title_fullStr Sugar microarray via click chemistry: molecular recognition with lectins and amyloid β (1–42)
title_full_unstemmed Sugar microarray via click chemistry: molecular recognition with lectins and amyloid β (1–42)
title_sort sugar microarray via click chemistry: molecular recognition with lectins and amyloid β (1–42)
publisher Taylor & Francis Group
series Science and Technology of Advanced Materials
issn 1468-6996
1878-5514
publishDate 2009-01-01
description Sugar microarrays were fabricated on various substrates via click chemistry. Acetylene-terminated substrates were prepared by forming self-assembled monolayers (SAMs) on a gold substrate with alkyl-disulfide and on silicon, quartz and glass substrates with a silane-coupling reagent. The gold substrates were subjected to surface plasmon resonance measurements, and the quartz and glass substrates were subjected to spectroscopy measurements and optical microscopy observation. The saccharide-immobilized substrate on the gold substrate showed specific interaction with the corresponding lectin, and the saccharides showed inert surface properties to other proteins with a high signal-to-noise ratio. We also focused on the saccharide–protein interaction on protein amyloidosis of Alzheimer amyloid β. Amyloid β peptide showed conformation transition on the saccharide-immobilization substrate into a β-sheet, and fibril formation and amyloid aggregates were found on the specific saccharides.
topic self-assembled monolayer
saccharide
microarray
surface plasmon resonance
amyloid
Alzheimer
url http://www.iop.org/EJ/abstract/1468-6996/10/3/034605
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