@misc{10481/71723,
year = {2022},
month = {1},
url = {http://hdl.handle.net/10481/71723},
abstract = {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).},
organization = {CBUA},
organization = {Spanish Ministerio de Educación y Formación},
organization = {Universidad de Granada},
organization = {European Regional Development Fund

104366RB-C22, 114256RB-I00, MCIN/AEI/10.13039/501100011033, PID2019, PID2019–104366RB-C22, PID2020, PID2020–114256RB-I00},
publisher = {Elsevier},
keywords = {Amyloid fibrils},
keywords = {Protein aggregation},
keywords = {Solvatochromic dyes},
keywords = {Biomarkers},
keywords = {FLIM},
keywords = {STED microscopy},
title = {A FRET pair for quantitative and superresolution imaging of amyloid  fibril formation},
doi = {10.1016/j.snb.2021.130882},
author = {Ruiz-Arias, Álvaro and Jurado Palomares, Rocío and Fueyo González, Francisco and Herranz, Rosario and Gálvez Rodríguez, Natividad and González Vera, Juan Antonio and Orte Gutiérrez, Ángel},
}