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  4. A synthetic membrane protein in tethered lipid bilayers for immunosensing in whole blood
 
research article

A synthetic membrane protein in tethered lipid bilayers for immunosensing in whole blood

Terrettaz, Samuel  
•
Follonier, Sylvain
•
Makohliso, Solomzi
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2009
Journal of Structural Biology

Tethered lipid bilayers, containing a transmembrane synthetic ligand-gated ion channel (SLIC), have been formed on gold surfaces. The SLIC was designed as a highly selective receptor and reporter protein to detect antibodies in whole blood, which are of importance in malaria diagnosis. The specific binding of the antibody to the sensor surface was monitored on-line with label-free surface-sensitive techniques either optically by surface plasmon resonance in whole blood or electrically by measuring the channel activity of SLIC in blood serum. We demonstrate the feasibility of a highly sensitive and easily applicable whole blood biosensor on the basis of simple commercially available components. The sensor might find applications in the field of infectious diseases such as point-of-care diagnostics of malaria, high content quality control of blood samples of donors, or monitoring the efficacy of vaccination. (C) 2009 Elsevier Inc. All rights reserved.

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Type
research article
DOI
10.1016/j.jsb.2009.03.011
Web of Science ID

WOS:000274799800019

Author(s)
Terrettaz, Samuel  
Follonier, Sylvain
Makohliso, Solomzi
Vogel, Horst  
Date Issued

2009

Publisher

Elsevier

Published in
Journal of Structural Biology
Volume

168

Issue

1

Start page

177

End page

182

Subjects

Biosensor

•

Impedance spectroscopy

•

Infectious diseases

•

Malaria

•

Surface plasmon resonance

•

Synthetic ion channel

•

Tethered membrane

•

Surface-Plasmon Resonance

•

Ion-Channel

•

Biomolecular Interactions

•

Biosensor Literature

•

Optical Biosensor

•

Gold Surfaces

•

Serum

•

Immunoassay

•

Melittin

•

Monolayers

Editorial or Peer reviewed

REVIEWED

Written at

EPFL

EPFL units
LCPPM  
Available on Infoscience
April 30, 2010
Use this identifier to reference this record
https://infoscience.epfl.ch/handle/20.500.14299/49873
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