Journal: In Silico Pharmacology

Article Title: Exploring Sm DHODH inhibition: natural products with potential anti-schistosomiasis activity

doi: 10.1007/s40203-026-00628-1

Figure Lengend Snippet: Overlay of the human DHODH enzyme and the S. mansoni enzyme to identify differences between the human (pink) and parasite (blue) structures. The protruding blue loop at the top of the structure corresponds to the potential site of Sm DHODH, which may coordinate the entry of compounds into the binding pocket. The presence of ten residues (Gly285 to Lys294) in the loop of binding site 2 (highly conserved across all species of the Schistosoma genus) allows for significant rearrangement in this region compared to other classes of DHODH structures

Article Snippet: Molecular dynamics analyses indicated that compound 3 induced significant conformational changes in the Sm DHODH structure, especially in the loop regions near the site 2, suggesting the enzyme’s structural flexibility upon binding with the ligand.

Techniques: Binding Assay

Journal: In Silico Pharmacology

Article Title: Exploring Sm DHODH inhibition: natural products with potential anti-schistosomiasis activity

doi: 10.1007/s40203-026-00628-1

Figure Lengend Snippet: a Three-dimensional representation of the Sm DHODH structure with emphasis on cluster 1. The regions in green correspond to the protein structure, while the orange areas represent the cavities identified from the analysis. Cluster 1 shows a connection between the active sites, suggesting potential interactions between these locations. b The yellow regions represent polar contacts of the binding sites, and the red regions indicate hydrophobic contacts.

Article Snippet: Molecular dynamics analyses indicated that compound 3 induced significant conformational changes in the Sm DHODH structure, especially in the loop regions near the site 2, suggesting the enzyme’s structural flexibility upon binding with the ligand.

Techniques: Binding Assay

Journal: In Silico Pharmacology

Article Title: Exploring Sm DHODH inhibition: natural products with potential anti-schistosomiasis activity

doi: 10.1007/s40203-026-00628-1

Figure Lengend Snippet: a Structure of the enzyme with the field of arrows, using mode 5, which show twisting or rotational movements between domains, domain bending, and global opening and closing movements; b representation of Sm DHODH in ball and stick model. Blue: regions with low B-factor values, meaning that the atoms in this area are more ordered or have lower mobility. Green and yellow: intermediate B-factor values. Red: regions with high B-factor values, suggesting more flexible or disordered atoms

Article Snippet: Molecular dynamics analyses indicated that compound 3 induced significant conformational changes in the Sm DHODH structure, especially in the loop regions near the site 2, suggesting the enzyme’s structural flexibility upon binding with the ligand.

Techniques:

Journal: In Silico Pharmacology

Article Title: Exploring Sm DHODH inhibition: natural products with potential anti-schistosomiasis activity

doi: 10.1007/s40203-026-00628-1

Figure Lengend Snippet: Results of the compounds docked at the biological receptor ( Sm DHODH) with the best poses obtained from the docking simulations at site 1, emphasizing hydrogen bonds with the residues in the selected site

Article Snippet: Molecular dynamics analyses indicated that compound 3 induced significant conformational changes in the Sm DHODH structure, especially in the loop regions near the site 2, suggesting the enzyme’s structural flexibility upon binding with the ligand.

Techniques:

Journal: In Silico Pharmacology

Article Title: Exploring Sm DHODH inhibition: natural products with potential anti-schistosomiasis activity

doi: 10.1007/s40203-026-00628-1

Figure Lengend Snippet: Results of the compounds 1–4 and PZQ docked to the biological receptor ( Sm DHODH) with the best poses obtained at the potential binding site. Hydrogen bonds with residues at site 2 are highlighted

Article Snippet: Molecular dynamics analyses indicated that compound 3 induced significant conformational changes in the Sm DHODH structure, especially in the loop regions near the site 2, suggesting the enzyme’s structural flexibility upon binding with the ligand.

Techniques: Binding Assay

Journal: In Silico Pharmacology

Article Title: Exploring Sm DHODH inhibition: natural products with potential anti-schistosomiasis activity

doi: 10.1007/s40203-026-00628-1

Figure Lengend Snippet: RMSD plots for the complexes formed between compound 3 and binding sites 1 ( a ) and 2 ( b ). The black lines represent the apo form of Sm DHODH, while the red lines correspond to the complexes formed with compound 3 at sites 1 ( a ) and 2 ( b )

Article Snippet: Molecular dynamics analyses indicated that compound 3 induced significant conformational changes in the Sm DHODH structure, especially in the loop regions near the site 2, suggesting the enzyme’s structural flexibility upon binding with the ligand.

Techniques: Binding Assay

Journal: In Silico Pharmacology

Article Title: Exploring Sm DHODH inhibition: natural products with potential anti-schistosomiasis activity

doi: 10.1007/s40203-026-00628-1

Figure Lengend Snippet: RMSF plots for the most stable structures of compound 3 at the binding sites 1 ( A ) and 2 ( B ) of the Sm DHODH enzyme

Article Snippet: Molecular dynamics analyses indicated that compound 3 induced significant conformational changes in the Sm DHODH structure, especially in the loop regions near the site 2, suggesting the enzyme’s structural flexibility upon binding with the ligand.

Techniques: Binding Assay

Journal: In Silico Pharmacology

Article Title: Exploring Sm DHODH inhibition: natural products with potential anti-schistosomiasis activity

doi: 10.1007/s40203-026-00628-1

Figure Lengend Snippet: Inhibition curves of Sm DHODH for compound 3 after incubation (0 and 2 h). The enzyme was incubated with different concentrations of compound 3, and the residual activity was measured

Article Snippet: Molecular dynamics analyses indicated that compound 3 induced significant conformational changes in the Sm DHODH structure, especially in the loop regions near the site 2, suggesting the enzyme’s structural flexibility upon binding with the ligand.

Techniques: Inhibition, Incubation, Activity Assay

Journal: In Silico Pharmacology

Article Title: Exploring Sm DHODH inhibition: natural products with potential anti-schistosomiasis activity

doi: 10.1007/s40203-026-00628-1

Figure Lengend Snippet: Molecular docking results of derivatives 3a, 3b, 3c, and 3d, highlighting hydrogen-bonding interactions with key residues (His50,Ser53, Tyr31, and Arg130) at site 1 of Sm DHODH

Article Snippet: Molecular dynamics analyses indicated that compound 3 induced significant conformational changes in the Sm DHODH structure, especially in the loop regions near the site 2, suggesting the enzyme’s structural flexibility upon binding with the ligand.

Techniques: