Aphis craccivora is an aphid which damages many species of plants, but with a higher predilection for beans, and is also a vector for numerous plant viruses. Therefore, to find potent and relatively safe insecticides against it may be a justified desideratum. Since neonicotinoids are a well-known class of effective insecticides with less toxicity against mammals and other vertebrates, a small dataset of compounds retrieved from literature based on similarity with highly active neoticotinoids was used. The dataset was preliminary investigated using the BeeTox tool to predict the bee toxicity of these compounds. They were found to be safe. In the absence of experimental data in silico approaches, such as molecular modelling methods, are considered to be reliable alternatives. Thus, homology modelling was involved for the building of the 3D structure of the acetylcholine receptor subunit alpha-L1 of Aphis craccivora based on the X-ray structure of human nicotinic acetylcholine receptor (PDB ID: 6PV7). The 3D structure of the obtained homology model is a dimer and the identified binding site is located between its two repeated units. After the refinement and evaluating steps, the homology model was involved in virtual screening experiments using the Fred docking tool of the OpenEye software. The aforementioned dataset was used to explore the intermolecular ligand-target interaction patterns for a rational design of desired insecticides. The hydrophobic interactions with the following amino acids of the binding site: Trp149, Trp59, Tyr190, Tyr197, Leu123, Ile113 were found to be the main ligand-protein binding mechanism.