Functional nicotinic acetylcholine receptor reconstitution in Au(111)-supported thiolipid monolayers.

PISSINIS, D.E.; DÍAZ, C. ; MAZA, E.; BONINI, I.C.; BARRANTES, F.J.; SALVAREZZA, R.C.; SCHILARDI, P.L.

Nanoscale

Royal Society of Chemistry

Lugar: Cambridge; Año: 2015 vol. 7 p. 15789 - 15797

2040-3364

The insertion and function of the muscle-typenicotinic acetylcholine receptor (nAChR) in Au(111)-supported thiolipidself-assembled monolayers has been studied by atomic force microscopy (AFM), surfaceplasmon resonance (SPR), and electrochemical techniques. It was possible forthe first time to resolve the supramolecular arrangement of the protein spontaneouslyinserted in a thiolipid monolayer in aqueous solution. Geometric supramoleculararrays of nAChRs were observed, most commonly in a triangular form compatiblewith three nAChR dimers of ~20 nm each. Addition of the full agonistcarbamoylcholine activated and opened the nAChR ion channel, as revealed by theincrease in capacitance relative to that of the nAChR-thiolipid system underbasal conditions. Thus, the self-assembled system appears to be a viable biomimeticmodel to measure ionic conductance mediated by ion-gated ion channels underdifferent experimental conditions, with potential applications in biotechnologyand pharmacology.