Molecular docking interactions of Parkinson's disease-linked alpha-synuclein with carbidopa, entacapone, and lauric acid : an in silico analysis

Date

6-2022

Degree

Bachelor of Science in Biology

College

College of Arts and Sciences (CAS)

Adviser/Committee Chair

Maria Claret L. Tsuchiya

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Abstract

Alpha-synuclein is a Parkinson’s Disease (PD)-linked protein that forms Lewy bodies upon aggregation. Characteristics of alpha-synuclein include its autophagy recognition motif and the acidic carboxyl terminus contributing to its chances of aggregation. Therapeutic drugs such as carbidopa and entacapone have been established for PD in the Philippines but no studies yet on the molecular docking of these medications as ligands to alpha-synuclein. In this study, in silico molecular docking simulation (SwissDock) was performed to assess the binding affinities of carbidopa, entacapone, and lauric acid, a common component of anti-neuro-inflammatory drugs. Analysis revealed hydrophilic interactions between the protein and the known medications, while hydrophobic interaction with lauric acid. The binding pocket of carbidopa was at the carboxyl domain of alpha-synuclein where serine and glutamic acid residues were concentrated. Entacapone and lauric acid were both bound to the autophagy recognition motif. Entacapone had the highest binding energy followed by lauric acid establishing the potential of lauric acid as a component for PD medication. The binding pocket and affinities of carbidopa and entacapone correlate with their action in preventing the aggregation of the protein serving as a basis for potential ligands to alpha-synuclein. These in silico results showing the direct interaction of lauric acid to alpha-synuclein through hydrophobic interaction msy provide structural and functional information for drug design involved in PD and other neurodegenerative diseases.

Language

English

LC Subject

Alpha-synuclein, Entacapone, Lauric acid, Parkinson's disease, Biology, Cell and Molecular Biology Institute of Biological Sciences

Location

UPLB Main Library Special Collections Section (USCS)

Call Number

LG 993.5 2022 B4 A53

Document Type

Thesis

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