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Object Prallethrin is a pyrethroid-based insecticide, commonly used as a liquid vaporizer in household, schools, and offices to repel mosquitoes. Due to worldwide application, human beings are exposed to this compound via inhalation. Inhalation of prallethrin can expose lung surfactant proteins (SPs) to this compound. SPs such as SP-A and SP-D have anti-microbial activities, whereas SP-B and SP-C prevent alveolar collapse during exhalation by reducing surface pressure in alveolar walls. The present study aimed to investigate the binding affinities of prallethrin for the pulmonary SPs and the possible interactions involved in it. Methods In this study, molecular docking was performed using prallethrin as ligand and lung SPs as target molecules. The three-dimensional structure of prallethrin (PubChem CID: 9839306) was retrieved from PubChem (https://pubchem.ncbi.nlm.nih.gov/), whereas the same for SPs were retrieved from RCSB Protein Data Bank (https://www.rcsb.org/). AutoDock 4.2 employing Lamarckian genetic algorithm was used to calculate binding affinities between the target protein and the ligand. Polar and nonpolar interactions between the amino acids of SPs and Prallethrin were studied utilizing Chimera X and Discovery Studio Visualizer. Results Results demonstrated that, prallethrin can bind with the four SPs using several interactions such as hydrogen bonds, alkyl bonds, Pi–Pi interaction, Van der Waals interaction and other. Prallethrin interacted with two binding pockets of SP-A and SP-C, whereas the prallethrin interacted with three binding pockets of SP-B and SP-D, respectively. Conclusion Findings of the study indicated that prallethrin can bind with the pulmonary SPs employing hydrogen and hydrophobic interactions. Such interactions could impair critical functions of SPs in lungs. This might increase susceptibility of lungs towards a range of respiratory illness, pathogenic infections, as well as malignancy. Graphical abstract