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Spatiotemporal formation of a single liquid-like condensate and amyloid fibrils of α-synuclein by optical trapping at solution surface.
Yuzu, Keisuke; Lin, Ching-Yang; Yi, Po-Wei; Huang, Chih-Hao; Masuhara, Hiroshi; Chatani, Eri.
Afiliación
  • Yuzu K; Department of Chemistry, Graduate School of Science, Kobe University, Kobe 657-8501, Japan.
  • Lin CY; Department of Applied Chemistry, National Yang Ming Chiao Tung University, Hsinchu 300093, Taiwan.
  • Yi PW; Department of Applied Chemistry, National Yang Ming Chiao Tung University, Hsinchu 300093, Taiwan.
  • Huang CH; Department of Applied Chemistry, National Yang Ming Chiao Tung University, Hsinchu 300093, Taiwan.
  • Masuhara H; Department of Applied Chemistry, National Yang Ming Chiao Tung University, Hsinchu 300093, Taiwan.
  • Chatani E; Department of Chemistry, Graduate School of Science, Kobe University, Kobe 657-8501, Japan.
Proc Natl Acad Sci U S A ; 121(39): e2402162121, 2024 Sep 24.
Article en En | MEDLINE | ID: mdl-39292741
ABSTRACT
Liquid-like protein condensates have recently attracted much attention due to their critical roles in biological phenomena. They typically show high fluidity and reversibility for exhibiting biological functions, while occasionally serving as sites for the formation of amyloid fibrils. To comprehend the properties of protein condensates that underlie biological function and pathogenesis, it is crucial to study them at the single-condensate level; however, this is currently challenging due to a lack of applicable methods. Here, we demonstrate that optical trapping is capable of inducing the formation of a single liquid-like condensate of α-synuclein in a spatiotemporally controlled manner. The irradiation of tightly focused near-infrared laser at an air/solution interface formed a condensate under conditions coexisting with polyethylene glycol. The fluorescent dye-labeled imaging showed that the optically induced condensate has a gradient of protein concentration from the center to the edge, suggesting that it is fabricated through optical pumping-up of the α-synuclein clusters and the expansion along the interface. Furthermore, Raman spectroscopy and thioflavin T fluorescence analysis revealed that continuous laser irradiation induces structural transition of protein molecules inside the condensate to ß-sheet rich structure, ultimately leading to the condensate deformation and furthermore, the formation of amyloid fibrils. These observations indicate that optical trapping is a powerful technique for examining the microscopic mechanisms of condensate appearance and growth, and furthermore, subsequent aging leading to amyloid fibril formation.
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Texto completo: 1 Colección: 01-internacional Base de datos: MEDLINE Asunto principal: Alfa-Sinucleína / Pinzas Ópticas / Amiloide Límite: Humans Idioma: En Revista: Proc Natl Acad Sci U S A Año: 2024 Tipo del documento: Article País de afiliación: Japón Pais de publicación: Estados Unidos
Texto completo
Añadir a Mi BVS
Imprimir
XML
PubMed Links
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Texto completo: 1 Colección: 01-internacional Base de datos: MEDLINE Asunto principal: Alfa-Sinucleína / Pinzas Ópticas / Amiloide Límite: Humans Idioma: En Revista: Proc Natl Acad Sci U S A Año: 2024 Tipo del documento: Article País de afiliación: Japón Pais de publicación: Estados Unidos