Sequences of the selected peptides, their codes, number of sequences and binding affinity from docking in kcal/mol.

Sequences of the selected peptides, their codes, number of sequences and binding affinity from docking in kcal/mol.</p

The structural of the <i>Lymnaea stagnalis</i> Acetylcholine-Binding Protein Q55R mutant complex (PDB ID 3WTH).

The structural of the Lymnaea stagnalis Acetylcholine-Binding Protein Q55R mutant complex (PDB ID 3WTH).</p

Fig 4 -

A) Chemical structure of the three neonicotinoid pesticides and B) Plots of root mean square deviation (RMSD) and the average free energy determined for the selectivity of WQA34 peptide (the error bars are obtained from three different trajectories). Figure (A) shows the 2D chemical structure of the three neonicotinoid pesticides IMI: imidacloprid, ACE: acetamiprid, CLT: Clothianidin and Figure (B) shows the plots of root mean square deviation (RMSD) in Å (grey color) and MM-PBSA results in kcal/mol with the error bars (green color) determined for the selectivity of WQA34 peptide.</p

The average free energies result in kcal/mol for the solvated systems, details of the energy contributions for the different complexes and the dissociation constant ^a.

The average free energies result in kcal/mol for the solvated systems, details of the energy contributions for the different complexes and the dissociation constant a.</p

Fig 3 -

The molecular dynamic results: A) the root mean square deviation (RMSD) for the free and the associated peptides, B) The root mean square deviation (RMSD) for the peptides vs time. (The root mean square deviation (RMSD) in Å for the five peptides YSM21, PSM22, PSW31, WQA34 and RNR1: the free peptides (in red color) and the associated peptides (in orange color); B) The root mean square deviation (RMSD) for these five peptides vs time in nano second).</p

S3 Fig -

A) The 3D-structure of RNR12 peptide B) The interactions between IMI and RNR12 ligand from molecular docking calculations. (DOCX)</p

3D structures for IMI and the four peptides YSM21, PSM22, PSW31, and WQA34.

In the middle is the structure of the IMI compound surrounded by four peptides YSM21, PSM22, PSW31, and WQA34 which have been obtained from the combination of the initial ones.</p

Fig 2 -

Interactions between IMI and a) YSM21, b) PSM22, c) PSW31 and d) WQA34 form the molecular docking results. The non-covalent interactions established between the IMI compound and the four peptides as the results of the molecular docking generated by BIOVIA Discovery Studio Visualizer software.</p

S2 Fig -

The 3D structures of the (A) position of IMI between chain A and chain B (B) interactions between IMI and the chain A and B residues. (DOCX)</p

S4 Fig -

A) The number of contacts for the peptides vs time B) The minimum number of contacts for each peptide. (DOCX)</p