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Related Experiment Video

Updated: Oct 16, 2025

Utilizing Time-Resolved Protein-Induced Fluorescence Enhancement to Identify Stable Local Conformations One α-Synuclein Monomer at a Time

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Published on: May 30, 2021

Structural and Functional Insights into α-Synuclein Fibril Polymorphism.

Surabhi Mehra¹, Laxmikant Gadhe¹, Riya Bera¹

¹Department of Biosciences and Bioengineering, IIT Bombay, Powai, Mumbai 400076, India.

|October 23, 2021

Summary

Alpha-synuclein (α-Syn) aggregation causes synucleinopathies like Parkinson's disease. Diverse α-Syn forms, similar to prions, explain varied disease presentations and pathology.

Keywords:

amyloid polymorphs synucleinopathies α-synuclein

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Atomic Scale Structural Studies of Macromolecular Assemblies by Solid-state Nuclear Magnetic Resonance Spectroscopy

Atomic Scale Structural Studies of Macromolecular Assemblies by Solid-state Nuclear Magnetic Resonance Spectroscopy

Published on: September 17, 2017

Area of Science:

Neuroscience
Biochemistry
Pathology

Background:

Abnormal alpha-synuclein (α-Syn) aggregation characterizes synucleinopathies, including Parkinson's disease (PD), multiple system atrophy (MSA), and dementia with Lewy bodies (DLB).
These diseases display clinical and pathological heterogeneity, mirroring prion disorders.
Emerging evidence points to α-Syn self-assembly into conformationally distinct polymorphs, akin to prions.

Purpose of the Study:

To review the clinical and pathological variability observed in synucleinopathies.
To explore the phenomenon of alpha-synuclein (α-Syn) fibril polymorphism.
To elucidate the structure-pathogenic relationship of α-Syn and its contribution to disease heterogeneity.

Main Methods:

Review of existing literature on synucleinopathies, α-Syn aggregation, and prion-like behavior.
Analysis of studies detailing α-Syn polymorphs, their structures, and in vivo/in vitro properties.
Examination of research linking α-Syn strains to distinct pathological phenotypes in animal models.

Main Results:

α-Syn can polymerize into conformationally diverse polymorphs, exhibiting strain-specific properties.
These distinct α-Syn strains can induce different pathological phenotypes upon inoculation.
High-resolution molecular structures and brain-derived α-Syn strains have been identified.

Conclusions:

The conformational diversity of α-Syn aggregates (polymorphs) is a key factor in the heterogeneity of synucleinopathies.
Understanding α-Syn polymorphism is crucial for deciphering the structure-pathogenic relationships in these neurodegenerative diseases.
This knowledge advances our comprehension of clinical variability and may inform future therapeutic strategies for synucleinopathies.