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 |
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Pages (from-to) | 588-589 |
Number of pages | 2 |
Journal | Chemistry Letters |
Volume | 37 |
Issue number | 6 |
DOIs | |
Publication status | Published - 2008 Jun 5 |
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ASJC Scopus subject areas
- Chemistry(all)
Cite this
Liposome immobilization on peptide-modified quartz crystal microbalance electrodes for kinetic analysis of interactions on membrane surfaces. / Kasuya, Yuzo; Ohtaka, Megumi; Tsukamoto, Kei; Ikeda, Yasuyuki; Matsumura, Kazunari.
In: Chemistry Letters, Vol. 37, No. 6, 05.06.2008, p. 588-589.Research output: Contribution to journal › Article
}
TY - JOUR
T1 - Liposome immobilization on peptide-modified quartz crystal microbalance electrodes for kinetic analysis of interactions on membrane surfaces
AU - Kasuya, Yuzo
AU - Ohtaka, Megumi
AU - Tsukamoto, Kei
AU - Ikeda, Yasuyuki
AU - Matsumura, Kazunari
PY - 2008/6/5
Y1 - 2008/6/5
N2 - 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.
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.
UR - http://www.scopus.com/inward/record.url?scp=48249101566&partnerID=8YFLogxK
UR - http://www.scopus.com/inward/citedby.url?scp=48249101566&partnerID=8YFLogxK
U2 - 10.1246/cl.2008.588
DO - 10.1246/cl.2008.588
M3 - Article
AN - SCOPUS:48249101566
VL - 37
SP - 588
EP - 589
JO - Chemistry Letters
JF - Chemistry Letters
SN - 0366-7022
IS - 6
ER -