همایش ملی بیوانفورماتیک ایران

صفحه اصلی / 4th international edition and 13th Iranian Conference on Bioinformatics

Identification of a natural specific inhibitor for Akt1 protein through molecular docking studies and evaluation of DFT calculations and molecular dynamics simulations

نویسندگان :

Forough Pakzadi¹ Yaghub Pazhang² Ebrahim Nemati-Kande³

1- Department of Biology, Faculty of Science, Urmia University, Urmia, Iran 2- Department of Biology, Faculty of Science, Urmia University, Urmia, Iran 3- Department of Physical Chemistry, Faculty of Chemistry, Urmia University, Urmia, Iran

کلمات کلیدی :

AKT1،Zingiberene،Quercetin،Molecular Docking،DFT

چکیده :

The protein kinase B (Akt1) is a pivotal component in cellular signaling pathways and the regulation of cancer-related processes, establishing it as a vital target for the development of innovative therapeutic agents[1]. This research examines natural inhibitors, including quercetin, resveratrol, and zingiberene, to assess their interactions with Akt1 using molecular docking and free energy calculations density functional theory (DFT)[2]. Molecular docking[3] analysis indicated that all three compounds possess the ability to bind to Akt1's allosteric site, with quercetin displaying the strongest interaction due to its lower binding energy and more stable hydrogen bonding. Detailed evaluation of van der Waals and electrostatic forces through DFT calculations identified these factors as critical to the stability of the complexes. Although resveratrol and zingiberene also demonstrated significant interactions with Akt1, their binding energies and complex stabilities were comparatively weaker than those of quercetin. These findings suggest that quercetin holds substantial promise as a natural inhibitor for Akt1 and could serve as a cornerstone for developing anticancer therapies derived from natural compounds. This study not only emphasizes the therapeutic potential of quercetin but also highlights the indispensable role of molecular modeling and DFT calculations in elucidating protein-ligand interactions. These discoveries provide a foundation for subsequent experimental research and practical innovations in drug design.