Liposome immobilization on peptide-modified quartz crystal microbalance electrodes for kinetic analysis of interactions on membrane surfaces

Yuzo Kasuya; Megumi Ohtaka; Kei Tsukamoto; Yasuyuki Ikeda; Kazunari Matsumura

doi:10.1246/cl.2008.588

Liposome immobilization on peptide-modified quartz crystal microbalance electrodes for kinetic analysis of interactions on membrane surfaces

Yuzo Kasuya, Megumi Ohtaka, Kei Tsukamoto, Yasuyuki Ikeda, Kazunari Matsumura

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

4 Citations (Scopus)

Abstract

In order to facilitate biosensor analyses of interactions on membrane surfaces, a method of immobilizing liposome using anchoring amphiphilic peptides was developed. Intact liposomes were immobilized stably on a quartz crystal microbalance electrode and were applied to a quantitative study of glycolipids-protein interactions.

Original language	English
Pages (from-to)	588-589
Number of pages	2
Journal	Chemistry Letters
Volume	37
Issue number	6
DOIs	https://doi.org/10.1246/cl.2008.588
Publication status	Published - 2008 Jun 5

ASJC Scopus subject areas

Chemistry(all)

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title = "Liposome immobilization on peptide-modified quartz crystal microbalance electrodes for kinetic analysis of interactions on membrane surfaces",

abstract = "In order to facilitate biosensor analyses of interactions on membrane surfaces, a method of immobilizing liposome using anchoring amphiphilic peptides was developed. Intact liposomes were immobilized stably on a quartz crystal microbalance electrode and were applied to a quantitative study of glycolipids-protein interactions.",

author = "Yuzo Kasuya and Megumi Ohtaka and Kei Tsukamoto and Yasuyuki Ikeda and Kazunari Matsumura",

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AU - Kasuya, Yuzo

AU - Ohtaka, Megumi

AU - Tsukamoto, Kei

AU - Ikeda, Yasuyuki

AU - Matsumura, Kazunari

PY - 2008/6/5

Y1 - 2008/6/5

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AB - In order to facilitate biosensor analyses of interactions on membrane surfaces, a method of immobilizing liposome using anchoring amphiphilic peptides was developed. Intact liposomes were immobilized stably on a quartz crystal microbalance electrode and were applied to a quantitative study of glycolipids-protein interactions.

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