Integrating docking and molecular dynamics approaches for a series of proline-based 2,5-diketopiperazines as novel αβ-tubulin inhibitors.
In this work, docking tools were utilized in order to study the binding properties of more than five hundred of proline-based 2,5-diketopiperazine in the binding site of αβ-tubulin. Results revealed that 20 compounds among them showed lower binding energies in comparison with Tryprostatin-A, a well known tubulin inhibitor and therefore could be potential inhibitors of tubulin. However, the precise evaluation of binding poses represents the similar binding modes for all of these compounds and Tryprostatin-A. Finally, the best docked complex was subjected to a 25 ns molecular dynamics simulation to further validate the proposed binding mode of this compound.
['Fani|Najmeh|N|', 'Bordbar|Abdol-Khalegh|AK|', 'Ghayeb|Yousef|Y|', 'Sepehri|Saghi|S|']
D020816:Amino Acid Motifs D001665:Binding Sites D054659:Diketopiperazines D006801:Humans D006860:Hydrogen Bonding D026121:Indole Alkaloids D062105:Molecular Docking Simulation D056004:Molecular Dynamics Simulation D008969:Molecular Sequence Data D010879:Piperazines D011392:Proline D011485:Protein Binding D017510:Protein Folding D017433:Protein Structure, Secondary D017434:Protein Structure, Tertiary D021122:Protein Subunits D055672:Static Electricity D013816:Thermodynamics D014404:Tubulin D050257:Tubulin Modulators
αβ-tubulin molecular dynamics simulation Tryprostatin diketopiperazine molecular docking