Contrary to humans, many animals, especially insects, rely heavily on the sense of smell to detect their foods, predators, mating partners and nesting sites. Odor molecules are chemicals, originating from a source. When such chemical compounds interact with odorant binding proteins (OBPs) and subsequently with the receptors associated with the insect nervous system, a cascade of reactions commences. In the present study, an in-silicoappraisal of a broad range of aphid repellent molecules was carried out in order to propose their mechanism of action at molecular level. Initially 3-D protein structure prediction of odorant binding proteins was carried out using SWISS model, Phyre2 and Modeller. The aphid repellent molecule E-beta-farnesene (a chemical compound used as ligand) was retrieved from PubChem. Physiochemical analyses carried out by Protparam revealed that OBPs are basic in nature with 9.30 isoelectric point (pI) and based on aliphatic index OBPs were found to be thermostable. Protein-ligand interaction was carried out with the help of Auto Dock Vina (ADV) tool that revealed complex interactions among ligand and proteins showing binding affinities by different bonds including hydrogen bonding, hydrophobic bonding, and elastic bonds. However, Phe230 residue in OBP of Apis gossypii showed interaction with ligand’s C9 atom via hydrogen bond having bond length of 3.04 Å. The use of new analogous for a wide range of aphid pests should be carried out in future studies.