Identification of novel inhibitor targeting Fyn kinase using molecular docking analysis.

Dharani Nedunchezhian,Kulanthaivel Langeswaran,Sundar Santhoshkumar

doi:10.6026/97320630015419

Dharani Nedunchezhian, Kulanthaivel Langeswaran + Show 1 more

Open Access

https://doi.org/10.6026/97320630015419

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Abstract

Identification of tyrosine Fyn kinase inhibitor is recognized as an effective and feasible therapeutic measure in reducing consequences of memory loss disorder Alzheimer's. The present investigation has been attempted with an objective to find out a novel potent inhibitor with similar homological structure to Fyn kinase using structure based in silico screening measure. Such derived structure was compared with natural data base pool and were systematically analyzed. Ligand based interaction was also tested and evaluated. We applied a molecular dynamic simulation technique to validate the stability of the identified complexes and to understand the ligand binding mechanism. Results provide information on the characteristics of novel and potent inhibitor for tyrosinase Fyn kinase protein so as to develop an innovative strategy to treat AD.

Highlights

Tyrosine Fyn Kinase is a determined protein factor involved in the activity of cell signaling pathway
Several earlier reports were demonstrated and evident that Tyrosine Fyn was recognized as driven force causing AD by interacting Amyloid B and Tau, conferring a novel therapeutic strategy to address and minimize the consequences of AD
Several studies were focused on inter linkage of Tyrosine Fyn Kinase protein with

Summary

Introduction

Tyrosine Fyn Kinase is a determined protein factor involved in the activity of cell signaling pathway. Unusual occurrence in the rate of activity of Fyn Kinase in signaling, render toxic substances, resulting chronic disorder such as Alzheimer's [1]. This played a crucial role in phosphorylation and anti-phosphorylation process and confers its intra molecular affinity [2], Cell adhesion, synaptic activity and signaling [3]. Regulation of Fyn activity was obviously studied in several types of signaling pathways [4]. Several studies were focused on inter linkage of Tyrosine Fyn Kinase protein with

Methods

Discussion

Conclusion