Ligand interaction with the purified serotonin transporter in solution and at the air/water interface.
The purified serotonin transporter (SERT) was spread at the air/water interface and the effects both of its surface density and of the temperature on its interfacial behavior were studied. The recorded isotherms evidenced the existence of a stable monolayer undergoing a lengthy rearrangement. SERT/ligand interactions appeared to be dependent on the nature of the studied molecules. Whereas an unrelated drug (chlorcyclizine) did not bind to the spread SERT, it interacted with its specific ligands. Compared to heterocyclic drugs, for which binding appeared to be concentration-dependent, a 'two-site' mechanism was evidenced for pinoline and imipramine.
Faivre
V
V
Laboratoire de Physico-Chimie des Surfaces, UMR CNRS 8612, 5 rue J-B. Clément, 92296, Châtenay-Malabry, France.
Manivet
P
P
Callaway
J C
JC
Airaksinen
M M
MM
Morimoto
H
H
Baszkin
A
A
Launay
J M
JM
Rosilio
V
V
D000388:Air; D001665:Binding Sites; D001692:Biological Transport; D002352:Carrier Proteins / Q000737:chemistry / Q000378:metabolism*; D004305:Dose-Response Relationship, Drug; D006801:Humans; D008024:Ligands; D008562:Membrane Glycoproteins / Q000737:chemistry / Q000378:metabolism*; D026901:Membrane Transport Proteins; D009419:Nerve Tissue Proteins; D050486:Serotonin Plasma Membrane Transport Proteins; D012996:Solutions; D013500:Surface Tension; D013694:Temperament; D014867:Water / Q000737:chemistry
D002352:Carrier Proteins; D008024:Ligands; D008562:Membrane Glycoproteins; D026901:Membrane Transport Proteins; D009419:Nerve Tissue Proteins; C493230:SLC6A4 protein, human; D050486:Serotonin Plasma Membrane Transport Proteins; D012996:Solutions; D014867:Water