PMID: 8600918Jan 1, 1996Paper

Bispecific antibody modification of nicotinic acetylcholine receptors for biosensing

Biosensors & Bioelectronics
S R ReikenH Sutisna

Abstract

Recent results show that bispecific antibodies can be used to tailor the selectivity of nicotinic acetylcholine receptors for biosensing purposes. The nicotinic acetylcholine receptors reconstituted in bilayer lipid membranes are inactivated when two bispecific antibodies, attached to the same receptor, bind to a single antigen molecule. Experiments with patch clamp recording equipment reveal that antigen levels of 10(-8) M completely and irreversibly inactivate small numbers of nicotinic acetylcholine receptors. This approach may lead to the construction of biosensors capable of detecting individual antibody-antigen (Ab-Ag) binding events.

References

Dec 7, 1977·Biochemical and Biophysical Research Communications·S L HamiltonA Karlin
Jan 1, 1992·Biosensors & Bioelectronics·R S SkeenC D Barnes
Feb 1, 1991·Immunology Today·M W FangerJ L Romet-Lemonne
Jan 1, 1983·Annual Review of Biophysics and Bioengineering·G P HessH Aoshima

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Citations

Jun 22, 2010·Current Opinion in Biotechnology·Sheereen MajdMichael Mayer
Jun 5, 1997·Nature·A P Turner
Jun 5, 1997·Nature·B A CornellR J Pace
Mar 19, 2005·Langmuir : the ACS Journal of Surfaces and Colloids·Emily L ChandlerDaniel L Burden

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