Structural Properties Study and Spectroscopic (FT-IR and UV-Vis) Profiling of the Novel Antagonist LY2157299 as a Transforming Growth Factor-β (TGF-β) Receptor I Kinase Inhibitor by Quantum-mechanical (QM) and Molecular Docking Techniques

Nabati, Mehdi; Sabahnoo, Hamideh; Lohrasbi, Elaheh; Mazidi, Mohammad

doi:10.22034/chemm.2018.149646.1093

Document Type : Original Article

Authors

¹ Synthesis and Molecular Simulation Laboratory, Chemistry Department, Pars Isotope Company, P.O. Box: 1437663181, Tehran, Iran

² Kit Formulation Laboratory, Radiopharmacy Department, Pars Isotope Company, P.O. Box: 1437663181, Tehran, Iran

³ Radiochemistry Laboratory, Quality Control (QC) Department, Pars Isotope Company, P.O. Box: 1437663181, Tehran, Iran

⁴ Biochemistry Laboratory, Quality Control (QC) Department, Pars Isotope Company, P.O. Box: 1437663181, Tehran, Iran

⁵ Faulty of Veterinary Medicine, University of Tehran, Tehran, Iran

10.22034/chemm.2018.149646.1093

Abstract

During the present study, the structural, vibrational, electronic and biological properties of the novel antagonist LY2157299 as a transforming growth factor-β (TGF-β) receptor I kinase inhibitor are explored by quantum-mechanical (QM) and molecular docking methods. The characterization of the title compound is done using FT-IR and UV-Vis spectroscopy methods. The above computations were carried out using density functional theory (B3LYP) method with 6-31+G(d,p) basis set. The frontier molecular orbitals (HOMO and LUMO) energies were used to calculate the global reactivity indices of the said compound. The results explored the stability, reactivity and bioactivity of the compound under study. To identify the nucleophilic and electrophilic sites in the said compound, the molecular electrostatic potential (MEP), electron localization function (ELF) and Mulliken charge distribution graphs were generated. The present paper further explains the ligand-protein interactions through molecular docking investigations. The results of the molecular docking studies indicate that the most important interactions between the ligand and protein are related to the residues His 285, Val 341, Lys 342, His 283 and Glu 284.

Graphical Abstract

Keywords

Main Subjects

Organic Chemistry

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Chemical Methodologies

Structural Properties Study and Spectroscopic (FT-IR and UV-Vis) Profiling of the Novel Antagonist LY2157299 as a Transforming Growth Factor-β (TGF-β) Receptor I Kinase Inhibitor by Quantum-mechanical (QM) and Molecular Docking Techniques

References

References

Volume 3, Issue 3
May and June 2019
Pages 377-391

Structural Properties Study and Spectroscopic (FT-IR and UV-Vis) Profiling of the Novel Antagonist LY2157299 as a Transforming Growth Factor-β (TGF-β) Receptor I Kinase Inhibitor by Quantum-mechanical (QM) and Molecular Docking Techniques

References

References

Volume 3, Issue 3May and June 2019Pages 377-391

Volume 3, Issue 3
May and June 2019
Pages 377-391