Intrinsically disordered proteins (IDPs) are proteins that lack a definitive secondary or tertiary structure. Due to their structural plasticity, flexible binding capability, and environmental sensitivity, IDPs can play diverse roles in modulation and regulation of their biological system. Under certain conditions, IDPs are prone to misfolding and aggregation, which are common traits in the pathology of neurodegenerative diseases. In Parkinson’s disease (PD) and related synucleinopathies, it is believed that the misfolding and aggregation of α-synuclein contributes to neurotoxicity. Along with their unique conformational dynamics, the biological behavior and function of IDPs such as α-synuclein are heavily influenced by post-translational modifications. Understanding how post-translational modifications affect the physiology and pathology of IDPs is essential for developing therapeutic and preventive strategies for neurodegenerative diseases. However, studying the site-specific effects of post-translational modifications can be challenging. By using chemical probes and semi-synthetic insertion techniques, the effects of post-translational modifications on aggregation, toxicity, and functional properties of α-synuclein can be characterized to unravel its role in PD. Furthermore, the study of these post-translational modifications can help identify new therapeutic targets to treat PD and IDP-related diseases.

Impact of post-translational modifications on the biophysical properties of α-synuclein: Implications to Parkinson's disease

Macromolecular Chemistry: The Second Century

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ACS Spring 2020 National Meeting & Expo

The official archive and repository for all ACS Meetings & Expositions abstracts and select posters or presentations.