Figure 6. Convergent high-affinity binding modes of top-performing Cu²⁺–peptide complexes in the catalytic groove of exo-β-(1,3)-glucanase. Surface representation of C. albicans exo-β-(1,3)-glucanase (green) with electrostatic potential mapped (red = anionic, blue = cationic). The two highest-ranking metallopeptide inhibitors—FLK12–Cu²⁺ (yellow sticks) and FLK6–Cu²⁺ (brown sticks)—are superposed within the catalytic groove, revealing convergent positioning within the anionic channel and extensive overlap of interaction hotspots. Metal coordination rigidifies the peptides and promotes deep penetration into the negatively charged pocket, enabling multi-point electrostatic anchoring and hydrogen-bond saturation consistent with the large affinity gains observed upon Cu²⁺ complexation. Cu²⁺ ions are shown as orange spheres : Docking-Based Evaluation of Defensin-Derived Peptides and Their Cu²⁺ Complexes as Dual-Target Inhibitors of Exo-β-(1,3)-Glucanase and Penicillin-Binding Protein Transglycosidase 1B : Science and Education Publishing

Figure 6. Convergent high-affinity binding modes of top-performing Cu²⁺–peptide complexes in the catalytic groove of exo-β-(1,3)-glucanase. Surface representation of C. albicans exo-β-(1,3)-glucanase (green) with electrostatic potential mapped (red = anionic, blue = cationic). The two highest-ranking metallopeptide inhibitors—FLK12–Cu²⁺ (yellow sticks) and FLK6–Cu²⁺ (brown sticks)—are superposed within the catalytic groove, revealing convergent positioning within the anionic channel and extensive overlap of interaction hotspots. Metal coordination rigidifies the peptides and promotes deep penetration into the negatively charged pocket, enabling multi-point electrostatic anchoring and hydrogen-bond saturation consistent with the large affinity gains observed upon Cu²⁺ complexation. Cu²⁺ ions are shown as orange spheres

American Journal of Pharmacological Sciences. 2026, 14(1), 7-19 doi:10.12691/ajps-14-1-2