Figure 1.
Various synthetic and natural insect repellents and attractants.
Figure 2.
Chemical structures of 43 carboxamides.
The most active compounds, with MED < 0.150 µmol/cm2, are marked with squares; the least active compounds, with MED > 5 µmol/cm2, are marked with circles.
Figure 3.
Chemical structures of 27 assorted compounds.
The most active compounds are marked with squares.
Figure 4.
MFTA model: (a) molecular super-graph, (b) factor dynamics, and (c) fit plot.
(a) The molecular supergraph is shown with two superimposed structures: DEET and N-cyclohexyl-N-ethyl-3-methylbutanamide (5m). The manner in which structures appear on MSG depends on how they can be superimposed onto the MSG as a whole. (b) The plot displays the change in correlation coefficient (R) and squared cross-validation coefficient (Q2) change as the number of factors changes. The best model is the one with the minimum possible number of factors and with R and Q2 at their highest values.
Figure 5.
Visualization of relative contributions of molecular fields to the title activity.
Positions discussed in the text are marked with arrows and boxed numbers; the six-membered ring (vertices 7 and 90-94) is encircled for clarity.
Figure 6.
2D predicted binding mode diagram for YF24 ((1S,2S)-2-phenylcyclohexanol).
2D protein-ligand interaction diagram generated using the Ligand Interaction script in Maestro (Schrödinger Inc., www.schrodinger.com). It outlines a highly hydrophobic cavity consisted of a number of proximate hydrophobic residues (shown in green circles) where YF24 binds. YF24 is represented as a 2D chemical sketch. A hydrogen bond between the ligand and Phe123 is shown by an arrow.
Figure 7.
3D predicted binding mode for YF24 ((1S,2S)-2-phenylcyclohexanol).
(B) Atomic details on how YF24 binds to OBP1, as depicted by ICM Browser (MolSoft, www.molsoft.com). An anchoring interaction that defines the position and orientation of the ligand is the hydrogen bond between the hydroxyl-group of YF24 and the backbone carbonyl group of Phe123. The rest of interaction is driven by a set of aromatic and hydrophobic residues, Phe59, Leu76, Trp114, Tyr122 and Phe123, that accommodates the cyclohexylbenzene core. Only proximate residues making contacts with YF24 are shown.
Figure 8.
Chemical structures of test set compounds.