Abstract
Parkinson’s disease is a common neurodegenerative disease. The differential expression of alpha-synuclein within Lewy Bodies leads to this disease. Some missense mutations of alpha-synuclein may resultant in functional aberrations. In this study, our objective is to verify the functional adaptation due to early and late-onset mutation which can trigger or control the rate of alpha-synuclein aggregation. In this regard, we have proposed a computational model to study the difference and similarities among the Wild type alpha-synuclein and mutants i.e., A30P, A53T, G51D, E46K, and H50Q. Evolutionary sequence space analysis is also performed in this experiment. Subsequently, a comparative study has been performed between structural information and sequence space outcomes. The study shows the structural variability among the selected subtypes. This information assists inter pathway modeling due to mutational aberrations. Based on the structural variability, we have identified the protein–protein interaction partners for each protein that helps to increase the robustness of the inter-pathway connectivity. Finally, few pathways have been identified from 12 semantic networks based on their association with mitochondrial dysfunction and dopaminergic pathways.
Highlights
Parkinson’s disease is a common neurodegenerative disease
It is known that α-Synuclein is the candidate protein of Parkinson’s disease
The family trait of the Synuclein family is analyzed in terms of order and disorder
Summary
Parkinson’s disease is a common neurodegenerative disease. The differential expression of alphasynuclein within Lewy Bodies leads to this disease. Our objective is to verify the functional adaptation due to early and late-onset mutation which can trigger or control the rate of alpha-synuclein aggregation. One of the common neurodegenerative disorders (NDs) is Parkinson’s disease (PD) which has been reported to be associated with the protein alpha-synuclein(Asyn)[1,2]. Phenotypical modifications can explain the internal orchestration of the pathways based on the mutated candidate and their interacting neighbors. These connections are observed for the mutated candidates by following the ancestral protein neighbors. One frame has been proposed by considering the sequential-structural modifications, and pathway semantics networks for Asyn and their mutants. The weight of the edges are computed based on the semantic similarities
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