Figure 8. Overall binding pose comparison of uncomplexed FLK11 with both target enzymes. (Top) Glucanase-bound FLK11 (cyan sticks) within the catalytic pocket of exo-β-(1,3)-glucanase (green surface). (Bottom) PBP1B-bound FLK11 (cyan sticks) within the transglycosylase groove of PBP1B (yellow surface). The peptide is well-fitted in the binding grooves of both proteins, adopting distinct conformations optimized for each active-site architecture. This dual behavior positions FLK11 as a versatile scaffold for pathogen-selective inhibitor development, with metal coordination functioning as a switchable modality that redirects target specificity

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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

Olatomide A. Fadare, Temitayo O. Aiyelabola, Imisioluwa A. Akintola, Janet I. Michael, Rachael Y. Fadare, Chiamaka V. Chukwu, Folakemi O. Yakubu, Deborah A. Sanni, Roheemah O. Lawal, Akitsu Takashiro, Adenike Kuku

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