Molecular Docking and Dynamics Simulation of Protein β-Tubulin and Antifungal Cyclic Lipopeptides

摘要: To elucidate interactions between the antifungal cyclic lipopeptides iturin A, fengycin, and surfactin produced by Bacillus bacteria microtubular protein β-tubulin in plant pathogenic fungi (Fusarium oxysporum, Colletrotrichum gloeosporioides, Alternaria alternata, Fusarium solani) molecular docking dynamics simulations, we retrieved structure of tubulin co-crystallized with taxol from Protein Data Bank (PDB) (ID: 1JFF) PubChem (Compound CID: 102287549, 100977820, 10129764). Similarity homology analyses those showed that conserved domains shared 84% similarity, root mean square deviation (RMSD) was less than 2 A. In studies, within binding pocket, residues Pro274, Thr276, Glu27 were responsible for interaction lipopeptides. analysis, two groups ligands formed based on number poses analyzed respect to RMSD. Group 1 made up 10, 100, 500 distances 0.080 0.092 nm RMSDs 0.10 0.15 nm. For group 2, consisting 1000 poses, initial final distance 0.1 range 0.30 These results suggest A fengycin bind higher affinity β-tubulin. may be used as lead compounds develop new agents or employed directly biorational products control fungi.