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...
| Authors: | ; ; ; ; ; ; ; ; ; ; ; |
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| Format: | Article |
| Status: | Published version |
| Publication date: | 2025 |
| Country: | España |
| Institution: | Varias* (Consorci de Biblioteques Universitáries de Catalunya, Centre de Serveis Científics i Acadèmics de Catalunya) |
| Repository: | Recercat. Dipósit de la Recerca de Catalunya |
| OAI Identifier: | oai:recercat.cat:2445/221379 |
| Online Access: | https://hdl.handle.net/2445/221379 |
| Access Level: | Open access |
| Keyword: | Amiloides Malària Plasmodium falciparum Amyloid Malaria |
| _version_ | 1878739636110491648 |
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| author | Espargaró Colomé, Alba |
| author2 | 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 |
| author2_role | author author author author author author author author author author author |
| author_browse | Arce, Elsa M. Busquets i Viñas, Ma. Antonia Domènech Cabrera, Òscar Espargaró Colomé, Alba Fernàndez Busquets, Xavier Gavín Marín, Rosalina Llabrés Prat, Salomé Luque Garriga, F. Xavier Muñoz-Torrero López-Ibarra, Diego Río Fernández, José Antonio del Sabaté Lagunas, Raimon Álvarez-Berbel, Irene |
| author_facet | 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 |
| author_role | author |
| collection | Recercat. Dipósit de la Recerca de Catalunya |
| description | 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. |
| eu_rights_str_mv | openAccess |
| format | article |
| id | ES_c53d61edc8b3e092ece7e5221e4e9176 |
| institution | Varias* (Consorci de Biblioteques Universitáries de Catalunya, Centre de Serveis Científics i Acadèmics de Catalunya) |
| instname_str | Varias* (Consorci de Biblioteques Universitáries de Catalunya, Centre de Serveis Científics i Acadèmics de Catalunya) |
| network_acronym_str | ES |
| network_name_str | España |
| oai_identifier_str | oai:recercat.cat:2445/221379 |
| publishDate | 2025 |
| publishDateSort | 2025 |
| publisher | Elsevier Ltd. |
| publisherStr | Elsevier Ltd. |
| reponame_str | Recercat. Dipósit de la Recerca de Catalunya |
| spelling | YAT2150: Overcoming limitations of traditional amyloid dyes in aggregation studies 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 Amiloides Malària Plasmodium falciparum Amyloid Malaria 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. Elsevier Ltd. https://hdl.handle.net/2445/221379 |
| spellingShingle | YAT2150: Overcoming limitations of traditional amyloid dyes in aggregation studies Espargaró Colomé, Alba Amiloides Malària Plasmodium falciparum Amyloid Malaria |
| status_str | publishedVersion |
| title | YAT2150: Overcoming limitations of traditional amyloid dyes in aggregation studies |
| title_full | YAT2150: Overcoming limitations of traditional amyloid dyes in aggregation studies |
| title_fullStr | YAT2150: Overcoming limitations of traditional amyloid dyes in aggregation studies |
| title_full_unstemmed | YAT2150: Overcoming limitations of traditional amyloid dyes in aggregation studies |
| title_short | YAT2150: Overcoming limitations of traditional amyloid dyes in aggregation studies |
| title_sort | YAT2150: Overcoming limitations of traditional amyloid dyes in aggregation studies |
| topic | Amiloides Malària Plasmodium falciparum Amyloid Malaria |
| topic_facet | Amiloides Malària Plasmodium falciparum Amyloid Malaria |
| url | https://hdl.handle.net/2445/221379 |