YAT2150: Overcoming limitations of traditional amyloid dyes in aggregation studies

Amyloid fibrils, which are aggregates of misfolded proteins characterized by β-sheet-rich structures, are implicated in several neurodegenerative and systemic pathologies, including Alzheimer’s and Parkinson’s diseases and type II diabetes mellitus. Traditional amyloid markers, such as Congo Red and...

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Detalles Bibliográficos
Autores: Espargaró Colomé, Alba, Álvarez-Berbel, Irene, Llabrés Prat, Salomé, Domènech Cabrera, Òscar, Busquets i Viñas, Ma. Antonia, Fernàndez Busquets, Xavier, Arce, Elsa M., Gavín Marín, Rosalina, Río Fernández, José Antonio del, Muñoz-Torrero López-Ibarra, Diego, Luque Garriga, F. Xavier, Sabaté Lagunas, Raimon
Tipo de recurso: artículo
Estado:Versión publicada
Fecha de publicación:2025
País:España
Institución:Universidad de Barcelona
Repositorio:Dipòsit Digital de la UB
OAI Identifier:oai:diposit.ub.edu:2445/221379
Acceso en línea:https://hdl.handle.net/2445/221379
Access Level:acceso abierto
Palabra clave:Amiloides
Malària
Plasmodium falciparum
Amyloid
Malaria
Descripción
Sumario:Amyloid fibrils, which are aggregates of misfolded proteins characterized by β-sheet-rich structures, are implicated in several neurodegenerative and systemic pathologies, including Alzheimer’s and Parkinson’s diseases and type II diabetes mellitus. Traditional amyloid markers, such as Congo Red and Thioflavin T, are widely used for amyloid detection but present limitations, particularly in cellular assays, due to spectral interference and aggregation inhibition. This study investigates YAT2150, a novel fluorescent dye with enhanced amyloid-binding specificity and sensitivity, as a potential alternative to conventional dyes. We evaluated YAT2150’s efficacy for detecting amyloid aggregates in both in vitro and in cellula assays. First, we compared its fluorescence intensity and binding specificity to that of Thioflavin T in amyloid fibril assays, demonstrating that YAT2150 exhibits high affinity and selectivity for amyloid structures, with minimal interference from non-aggregated proteins. Furthermore, we explored YAT2150’s utility in Escherichia coli as a model system for studying protein aggregation and amyloid formation in a procaryotic cellular context. Our findings indicate that YAT2150 effectively labels amyloid-like inclusion bodies in E. coli, producing a robust fluorescence signal with low background noise. These results suggest that YAT2150 is a promising new tool for amyloid research, offering greater sensitivity compared to traditional dyes, even in complex cellular environments.