Sudeepa Srichandan¹, Kripa N Nand²* , Amulya K Panda¹* and Pratima Ray³

¹Product Development Cell, National Institute of Immunology, Aruna Asaf Ali Marg, New Delhi, India

³Faculty of Science, Jamia Hamdard University, New Delhi, India

*Corresponding Author:Amulya K Panda and Kripa N Nand, Product Development Cell, National Institute of Immunology, Aruna Asaf Ali Marg, New Delhi, India and Department of Biological Sciences, RPI, New York, USA.

Received: March 03, 2022; Published: March 24, 2022

Abstract

α-synuclein (SNCA gene) aggregation in neuronal cells causes Parkinson’s disease (PD), one of the most common neurodegenerative diseases. Mutations in the SNCA gene locus and accumulation of metal ions are the major hallmarks in PD patients. Inclusion bodies of α-synuclein were expressed in E. coli by incorporating mutations in α-synuclein and supplementing metal ions in the culture media. The inclusion body aggregates were purified and analyzed for the presence of amyloid type structures using thioflavin binding. The structure and functional characteristics of inclusion body aggregates formed during protein expression in E. coli makes them a suitable model to understand the mechanism of amyloid formation. Soluble α-synuclein was aggregated to form amyloid type aggregates in vitro. Inclusion bodies of α-synuclein showed similar structure and similar kinetics of formation as that of in vitro aggregates of α-synuclein. Formation of α-synuclein as inclusion bodies in E. coli and its amyloidogenic characteristics can be used to understand the process of protein aggregation. This information will be useful in discovery of next generation inhibitors for Parkinson’s disease.

Keywords: α-synuclein; Aggregation; Inclusion Body; Amyloids; Parkinson’s Disease

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Citation

Citation: Amulya K Panda., et al. “Expression and Characterization of in vitro Aggregates and Inclusion Bodies of α-synuclein in E. coli". Acta Scientific Microbiology 5.4 (2022): 134-145.

Copyright

Copyright: © 2022 Amulya K Panda., et al. This is an open-access article distributed under the terms of the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original author and source are credited.