On a chip demonstration of a functional role for Odorant Binding Protein in the preservation of olfactory receptor activity at high odorant concentration.

The molecular mechanisms underlying odorant detection have been investigated using the chip based SPR technique by focusing on the dynamic interactions between transmembrane Olfactory Receptor OR1740, odorant ligands and soluble Odorant-Binding Protein (OBP-1F). The OR1740 present in the lipid bilayer of nanosomes derived from transformed yeasts specifically bound OBP-1F. The receptor preferential odorant ligand helional released bound OBP-1F from the OR-OBP complex, while unrelated odorants failed to do so. OBP-1F modified the functional OR1740 dose-response to helional, from a bell-shaped to a saturation curve, thus preserving OR activity at high ligand concentration. This unravels an active role for OBPs in olfaction, in addition to passive transport or a scavenger role. This sensorchip technology was applied to assessing native OBP-1F in a biological sample: rat olfactory mucus also displayed significant binding to OR1740 nanosomes, and the addition of helional yielded the dissociation of mucus OBP from the receptor.