Figure 7. Binding modes of top-performing uncomplexed FLK peptides in the PBP1B transglycosylase groove. Representative docking poses of FLK5 (cyan) and FLK13 (magenta) within the hydrophobic transglycosylase channel of penicillin-binding protein 1B (PBP1B). Both peptides adopt extended conformations that enable deep penetration into the narrow binding groove and establish a balanced interaction network combining hydrogen bonding and hydrophobic pocket occupation. The superposed poses illustrate how uncomplexed FLK peptides can conformationally adapt to the constrained topology of the PBP1B active site, providing a structural rationale for their superior binding relative to the rigid Cu²⁺–peptide complexes, which are sterically excluded from this pocket : 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 7. Binding modes of top-performing uncomplexed FLK peptides in the PBP1B transglycosylase groove. Representative docking poses of FLK5 (cyan) and FLK13 (magenta) within the hydrophobic transglycosylase channel of penicillin-binding protein 1B (PBP1B). Both peptides adopt extended conformations that enable deep penetration into the narrow binding groove and establish a balanced interaction network combining hydrogen bonding and hydrophobic pocket occupation. The superposed poses illustrate how uncomplexed FLK peptides can conformationally adapt to the constrained topology of the PBP1B active site, providing a structural rationale for their superior binding relative to the rigid Cu²⁺–peptide complexes, which are sterically excluded from this pocket

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