Residual Exploration into Apoptosis of Leukemic Cells Through Oncostatin M: A Computational Structural Oncologic Approach

  • Arundhati Banerjee
  • Rakhi DasguptaEmail author
  • Sujay RayEmail author
Conference paper
Part of the Advances in Intelligent Systems and Computing book series (AISC, volume 988)


Oncostatin M (OSM) targets cells through the formation of a triple protein complex involving gp130 and OSMR (oncostatin M receptor). This leads to sequential triggering of Jak/STAT pathways. Signal transduction thus occurs efficiently for the apoptosis of leukemic cells. In this study, the essential 3D protein structures were docked among themselves to form the trio-protein complex. Through optimization techniques upon the best docked structure, a comparative analysis was undergone to examine the stable conformation and firm interactive complex. Residual investigation through binding patterns if not performed, void remains in the research as efficient drug targeting holds a risk. ΔG values and other stability parameters inferred with a steadier and more spontaneous interaction to occur for the optimized protein complex. Gp130 showed an improvement in β-sheet formation via compromising coil-like conformation. Glu and Asp residues from OSMR protein formed more than 50% of ionic bonds with gp130 and OSM. OSMR acted as a linker peptide between OSM and gp130 (which formed one ionic interaction with OSM). Several Phe-Phe aromatic interactions were accomplished by OSMR to render an additional strength. Phe4 and Phe7 from OSMR played a double role through aromatic–aromatic and cation-pi interactions. Above 83% of cation-pi interactions were exhibited by OSMR protein. Altogether, all statistically validated evaluations affirmed the optimized protein complex to be the more stable and firmer one. This study possesses a foundation through molecular-level computational approach in oncology for the apoptosis of human leukemic cells. It would additionally instigate the drug discovery centered research.


Leukemic cells Oncostatin M Protein–protein interactions ΔG values Binding patterns Statistical significances 



High gratefulness is rendered to the Department of Biochemistry and Biophysics, University of Kalyani for the support. Authors render their gratefulness to DST PURSE (II) and DST-FIST program in the University of Kalyani. Authors are also grateful to the Department of Biotechnology, Amity University, Kolkata for the cooperation and support as well.

Conflicts of Interest



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© Springer Nature Singapore Pte Ltd. 2020

Authors and Affiliations

  1. 1.Department of Biochemistry and BiophysicsUniversity of KalyaniKalyani, NadiaIndia
  2. 2.Amity Institute of Biotechnology, Amity UniversityKolkataIndia

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