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Related Experiment Video

Updated: Mar 18, 2026

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

Versatile Structures of α-Synuclein.

Chuchu Wang¹, Chunyu Zhao¹, Dan Li¹

¹Interdisciplinary Research Center on Biology and Chemistry, Shanghai Institute of Organic Chemistry, Chinese Academy of Sciences Shanghai, China.

Frontiers in Molecular Neuroscience

|July 6, 2016

Summary

This summary is machine-generated.

Alpha-synuclein (α-syn) aggregation into Lewy bodies is key to Parkinson's disease (PD). This review explores α-syn's diverse structures and roles in neuronal function and PD pathogenesis.

Keywords:

Parkinson’s disease amyloid atomic structure protein aggregation vesicle trafficking α-synuclein

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Generation of Alpha-Synuclein Preformed Fibrils from Monomers and Use In Vivo

Generation of Alpha-Synuclein Preformed Fibrils from Monomers and Use In Vivo

Published on: June 2, 2019

Area of Science:

Neuroscience
Molecular Biology
Biochemistry

Background:

Alpha-synuclein (α-syn) is an intrinsically disordered protein found in presynaptic terminals.
α-syn aggregation into Lewy bodies (LB) is a hallmark of Parkinson's disease (PD).
α-syn exhibits significant conformational diversity, influencing its function and toxicity.

Purpose of the Study:

To review recent discoveries on α-syn structures under various conditions.
To elucidate the molecular mechanisms of α-syn transformation.
To understand the relationship between α-syn structural species, neuronal function, and PD pathogenesis.

Main Methods:

Literature review of recent studies on α-syn structure.
Analysis of α-syn conformations in membrane-bound, cytosolic, and amyloid states.
Integration of knowledge on α-syn structure-function and structure-pathology relationships.

Main Results:

α-syn exists in diverse structural forms, including membrane-bound, cytosolic, and amyloid states.
These structural variations are linked to α-syn's physiological functions and pathological roles.
Understanding these states is crucial for deciphering α-syn toxicity in PD.

Conclusions:

The conformational plasticity of α-syn is central to its dual role in neuronal health and disease.
Further research into α-syn structural dynamics can reveal insights into Parkinson's disease mechanisms.
Targeting specific α-syn conformations may offer therapeutic strategies for PD.