Abstract:
Parkinson’s disease (PD) is an idiopathic neurodegenerative disorder targeting seven to ten million of the elderly population. The PARK7 mutation trigger the loss of DJ-1 protein leading towards the early onset of PD.
Objective: Our study aims to identify the PARK7 protein interactions and its potent interacting inhibitor by implying various bioinformatic tools.
Methodology: In the present study, expression analysis was performed to determine the PARK7 gene expression levels in the CSF of PD patients. Then a detail spectrum analysis was performed for the quantification of the PARK7 protein fragment. Further, the ligand interactions of the PARK7 protein and α-synuclein were studied through LIGPLOT. Several bioinformatic tools were employed to study the protein-protein interactions along with post-translational modifications. Lastly, the technique of molecular docking was implied to detect the potent MAO-B inhibitor of the PARK7 protein.
Results: Our study demonstrated modified expression levels of the PARK7 protein. The PARK7 expression analysis displayed the P value of 0.0106 in healthy versus sporadic PD. While healthy versus genetic PD exhibited the P value of 0.0013. Our detailed spectrum analysis illustrated 13 percent sequence coverage for the PARK7_HUMAN across the MS sample. Further, this research introduced three biological replicates: (K) VTVAGLAGK(D);(K) VTTHPLAK(D)& (K) DGLILTSR(G) with 100%; 99%& 99% probabilities, respectively. Moreover, the docking results suggested Safinamide with -5.4492 best energy score to be more potent interacting inhibitor as compared to Selegiline and Rasagiline.
Conclusion: Outcome of this study, offers early characterization and targeting of proteins enabling effective diagnosis of PD. These investigations will aid in the discovery of alpha synuclein and MAO-B related inhibitors which reduced the effects of PD triggered by the PARK7 protein.
