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TitleSingle-Molecule Insight Into α-Synuclein Fibril Structure and Mechanics Modulated by Chemical Compounds.
Journal, issue, pagesAdv Sci (Weinh), Vol. 12, Issue 14, Page e2416721, Year 2025
Publish dateFeb 14, 2025
AuthorsXiang Li / Lulu Bi / Shenqing Zhang / Qianhui Xu / Wencheng Xia / Youqi Tao / Shaojuan Wu / Yanan Li / Weidong Le / Wenyan Kang / Dan Li / Bo Sun / Cong Liu /
PubMed Abstractα-Syn fibrils, a key pathological hallmark of Parkinson's disease, is closely associated with disease initiation and progression. Several small molecules are found to bind or dissolve α-syn ...α-Syn fibrils, a key pathological hallmark of Parkinson's disease, is closely associated with disease initiation and progression. Several small molecules are found to bind or dissolve α-syn fibrils, offering potential therapeutic applications. Here, an innovative optical tweezers-based, fluorescence-combined approach is developed to probe the mechanical characteristics of α-syn fibrils at the single-molecule level. When subjected to axial stretching, local deformation within α-syn fibrils appeared at forces above 50 pN. These structural alternations occurred stepwise and are irreversible, suggesting unfolding of individual α-syn molecules or subdomains. Additionally, α-syn fibrils exhibits high heterogeneity in lateral disruption, with rupture force ranging from 50 to 500 pN. The impact of different compounds on the structure and mechanical features of α-syn fibrils is further examined. Notably, epigallocatechin gallate (EGCG) generally attenuates the rupture force of fibrils by wedging into the N-terminal polar groove and induces fibril dissociation. Conversely, copper chlorophyllin A (CCA) attaches to four different sites wrapping around the fibril core, reinforcing the stability of the fibril against rupture forces. The work offers an effective method for characterizing single-fibril properties and bridges compound-induced structural alternations with mechanical response. These insights are valuable for understanding amyloid fibril mechanics and their regulation by small molecules.
External linksAdv Sci (Weinh) / PubMed:39951335 / PubMed Central
MethodsEM (helical sym.)
Resolution3.1 Å
Structure data

38733

8xwd

EMDB-38733, PDB-8xwd:
Croy-EM structure of alpha synuclein fibril with EGCG
Method: EM (helical sym.) / Resolution: 3.1 Å

Chemicals

ChemComp-KDH:
(2R,3R)-5,7-dihydroxy-2-(3,4,5-trihydroxyphenyl)-3,4-dihydro-2H-chromen-3-yl 3,4,5-trihydroxybenzoate

Source
  • homo sapiens (human)
KeywordsPROTEIN FIBRIL / amyloid

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