Acta Scientific Pharmaceutical Sciences (ASPS)(ISSN: 2581-5423)

Research Article Volume 5 Issue 11

In silico Evaluation of Solanine Compound as New Potential Inhibitors of Cancer Causing Enzymes

Rajalakshmi A1* and Jayachitra A2

1Assistant Professor, Department of Biotechnology, Sri Kaliswari College (Autonomous), Sivakasi, India
2Assistant Professor, Department of Plant Biotechnology, School of Biotechnology, Madurai Kamaraj University, Madurai, India

*Corresponding Author: Rajalakshmi A, Assistant Professor, Department of Biotechnology, Sri Kaliswari College (Autonomous), Sivakasi, India.

Received: August 24, 2021; Published: October 11, 2021



Explore the interaction mode and binding orientation of lead compound with target proteins by molecular docking studies and understand the structural insights and functional properties of potent target protein by autodock tools. Aim of this study to analyze the interaction of Solanine with cancer causing enzymes. Cyclin-dependent kinase 6, Cytochrome P450, Topoisomerase I, Topo IIa ATPase, anti-apoptotic protein Bcl-2 and Vegfr2 are critical molecules that control cell cycle progression from one phase to the other. However, mutational changes in these molecules lead to the purturbed cell cycle leading to uncontrolled cellular proliferation or cell death. Docking pose is almost close to the substrates for most of the receptors. Remarkably 1t8i - Topoisomerase I and 1zxm - TopoIIa ATPase docking was completely blocking the binding of the substrate with high affinity by the action of Solanine. The molecular docking was applied to explore the binding mechanism and to correlate its docking score with the activity of plant derived compounds.

Keywords: Solanine; Auotdock; Topoisomerase; Molecular Docking; Cell Cycle



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Citation: Rajalakshmi A and Jayachitra A. “In silico Evaluation of Solanine Compound as New Potential Inhibitors of Cancer Causing Enzymes". Acta Scientific Pharmaceutical Sciences 5.11 (2020): 20-23.


Acceptance rate32%
Acceptance to publication20-30 days

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