title: Analysis of the molecular interactions of the potent analgesic S1RA with the σ1 receptor.
abstract: The highly selective σ1 receptor antagonist S1RA is endowed with a surprisingly high affinity for its target protein given a missing fundamental hydrophobic pharmacophoric requirement. Here we show that, with respect to other potent σ1 ligands, S1RA is able to compensate this loss by fulfilling all other pharmacophoric requirements and by gaining in solvation energy.
authors.affiliation: Molecular Simulation Engineering (MOSE) Laboratory - DEA, University of Trieste, Piazzale Europa 1, 34127 Trieste, Italy.
authors.forename: Erik
authors.initials: E
authors.lastname: Laurini
authors.forename: Valentina
authors.initials: V
authors.lastname: Da Col
authors.forename: Bernhard
authors.initials: B
authors.lastname: Wünsch
authors.forename: Sabrina
authors.initials: S
authors.lastname: Pricl
mesh_terms: D008024:Ligands; D008958:Models, Molecular; D015394:Molecular Structure; D009025:Morpholines / Q000737:chemistry / Q000494:pharmacology*; D011720:Pyrazoles / Q000737:chemistry / Q000494:pharmacology*; D017480:Receptors, sigma / Q000037:antagonists & inhibitors*
chemical_list: C576663:4-(2-((5-methyl-1-(2-naphthalenyl)-1H-pyrazol-3-yl)oxy)ethyl)morpholine; D008024:Ligands; D009025:Morpholines; D011720:Pyrazoles; D017480:Receptors, sigma