Abstract
Precise estrus detection in sows is pivotal in increasing the productivity within the pork industry. Sows in estrus exhibit exclusive behaviors when exposed to either a live boar or the steroid pheromones androstenone and androstenol. Recently, a study employing solid-phase microextraction-gas chromatography-mass spectrometry has identified a novel salivary molecule in boars, known as quinoline. This finding has intriguing implications as a synthetic mixture of androstenone, androstenol, and quinoline induces estrus behaviors in sows. Nevertheless, the precise pheromonal characteristics of quinoline remain elusive. In this study, we validate and compare the binding efficiency of androstenone, androstenol, and quinoline with porcine olfactory receptor proteins (odorant-binding protein [OBP], pheromaxein, salivary lipocalin [SAL], and Von Ebner's gland protein [VEGP]) using molecular docking and molecular dynamics simulations. All protein-ligand complexes demonstrated stability, as evidenced by the root-mean-square deviation (RMSD), root-mean-square fluctuation (RMSF), radius of gyration (R(g)), solvent-accessible surface area (SASA), and hydrogen-bond (H-bond) plots. Furthermore, quinoline displayed higher binding efficiency with OBP, measured at -85.456 ± 8.268 kJ/mol, compared to androstenone and androstenol, as determined by molecular mechanics-Poisson-Boltzmann surface area (MM-PBSA) calculations. Conversely, quinoline exhibited a lower binding efficacy when interacting with SAL, pheromaxein, and VEGP compared to androstenone and androstenol. These findings, in part, suggest the binding possibility of quinoline with carrier proteins and warrant further investigation to support the role of quinoline in porcine chemical communication.