Benzyl alcohol synergistic effect with deltamethrin against Musca domestica with molecular docking of potential modes of action

The house fly (Musca domestica Linnaeus, 1758) has developed resistance to several pesticides, necessitating innovative approaches for effective control. This study explores the synergistic effects of benzyl alcohol (BA) on the toxicity of deltamethrin (D) against various life stages of M. domestica larvae, pupae, and adults. Additionally, molecular docking analyses were conducted to investigate interactions with the acetylcholinesterase enzyme (AChE) and voltage-sensitive sodium channel (Vssc). Two formulations of deltamethrin were tested: DBA mix (D 5% dissolved in ethyl alcohol, then mixed with BA at its LC50 concentration) and DBA combination (D 5% dissolved directly in pure BA). In vitro testing revealed significant synergistic effects. For larvae, the LC50 of deltamethrin alone was 0.95 mg/mL, while the DBA mix reduced it to 0.09 mg/mL, yielding a synergism factor of 10.56. For pupae, deltamethrin’s LC50 was 1.32 mg/mL, compared to 0.104 mg/mL for the DBA mix, with a synergism fac..., Statistics of the work
Ten replicates were performed for each treatment, and the results were expressed as mean ± standard error (SE). Analysis of variance (ANOVA) was used to analyze larval mortality data, and Duncan's multiple range tests (p < 0.05) were applied to compare the means. Probit analysis, as described by Finney (1952), was employed to determine the lethal concentrations (LC50 and LC90) and their corresponding 95% confidence limits. All statistical analyses were conducted using SPSS for Windows (version 22.0)., , # Data from: Benzyl alcohol synergistic effect with deltamethrin against Musca domestica with molecular docking of potential modes of action

Dataset DOI: [10.5061/dryad.12jm63z79](10.5061/dryad.12jm63z79)

## Description of the data and file structure

#### File: Supplemetary_fig_A.jpg and Supplemetary_fig_B.jpeg

**Description:** Figure S1. The secondary structure representation using SOPMA online website. The black letters represent the one letter abbreviation of the enzyme’s amino acid sequence, (h) in blue represents the amino acid residues forming alpha helix secondary structure, (c) in orange represents random coils, (e) in red is for extended strands, and (t) in green for beta turn secondary structures. The highest percentage is for Random coil (shown in orange) with a percentage of 50.89% followed by Alpha helix (Hh) (30.78%), then Extended strand (14.45%) and Beta turn (3.90%). *M. domestica* Acetylcholineesterase (AChE) sequence and their secondary structure representation (A...,