A FRET pair for quantitative and superresolution imaging of amyloid fibril formation
Metadatos
Mostrar el registro completo del ítemAutor
Ruiz-Arias, Álvaro; Jurado Palomares, Rocío; Fueyo González, Francisco; Herranz, Rosario; Gálvez Rodríguez, Natividad; González Vera, Juan Antonio; Orte Gutiérrez, ÁngelEditorial
Elsevier
Materia
Amyloid fibrils Protein aggregation Solvatochromic dyes Biomarkers FLIM STED microscopy
Fecha
2022-01-01Referencia bibliográfica
Ruiz-Arias, Á., Jurado, R., Fueyo-González, F., Herranz, R., Gálvez, N., González-Vera, J. A., & Orte, A. (2022). A FRET pair for quantitative and superresolution imaging of amyloid fibril formation. Sensors and Actuators B: Chemical, 350, 130882. [https://doi.org/10.1016/j.snb.2021.130882]
Patrocinador
CBUA; Spanish Ministerio de Educación y Formación; Universidad de Granada; European Regional Development Fund 104366RB-C22, 114256RB-I00, MCIN/AEI/10.13039/501100011033, PID2019, PID2019–104366RB-C22, PID2020, PID2020–114256RB-I00Resumen
The presence of neuritic plaques and amyloid fibrils arising from the misfolding of certain proteins is the principal molecular indicator of neurodegenerative diseases such as Alzheimer's and Parkinson's disease. Methodologies for studying the early stages of amyloid aggregation are rapidly arising to provide a better understanding of the mechanism of fibrillization and cytotoxicity and to identify potential targets for diagnosis and therapy. The method presented here involves the simultaneous use of two different fluorophores, a quinolimide derivative and Nile Blue A. These are capable of interacting with and reporting on the formation of preamyloid aggregates and fibrils of apoferritin through fluorescence resonance energy transfer (FRET), which occurs between them, thus maximizing the contrast in detection and quantitative information of such amyloid species by using multidimensional fluorescence lifetime imaging microscopy (FLIM).