Bispecific antibody modification of nicotinic acetylcholine receptors for biosensing.
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.
Reiken
S R
SR
Department of Chemical Engineering, Washington State University, Pullman 99164-2710, USA.
Van Wie
B J
BJ
Sutisna
H
H
D000818:Animals; D018033:Antibodies, Bispecific / Q000096:biosynthesis; D000911:Antibodies, Monoclonal / Q000096:biosynthesis; D015374:Biosensing Techniques; D002417:Cattle; D004557:Electric Organ / Q000378:metabolism; D005069:Evaluation Studies as Topic; D051379:Mice; D018733:Nicotinic Antagonists; D051381:Rats; D011978:Receptors, Nicotinic / Q000276:immunology* / Q000378:metabolism; D014101:Torpedo
D018033:Antibodies, Bispecific; D000911:Antibodies, Monoclonal; D018733:Nicotinic Antagonists; D011978:Receptors, Nicotinic