Specific interactions between mycobacterial FtsZ protein and curcumin derivatives: Molecular docking and ab initio molecular simulations

Highlights: • We study interactions of filamentous temperature-sensitive Z (FtsZ) with curcumin. • Protein-ligand docking, classical MM and ab initio fragment MO methods are used. • Curcumin derivatives prefer to bind the TZT-binding site of FtsZ. • Curcumin-III binds more strongly to FtsZ than the other curcumins. • The central carbonyl groups of curcumin-III form hydrogen bonds with FtsZ. Filamentous temperature-sensitive Z (FtsZ) protein plays essential role in bacteria cell division, and its inhibition prevents Mycobacteria reproduction. Here we adopted curcumin derivatives as candidates of novel inhibitors and investigated their specific interactions with FtsZ, using ab initio molecular simulations based on protein–ligand docking, classical molecular mechanics and ab initio fragment molecular orbital (FMO) calculations. Based on FMO calculations, we specified the most preferable site of curcumin binding to FtsZ and highlighted the key amino acid residues for curcumin binding at an electronic level. The result will be useful for proposing novel inhibitors against FtsZ based on curcumin derivatives.