@misc{10481/28515,
year = {2012},
url = {http://hdl.handle.net/10481/28515},
abstract = {Amyloidogenic protein aggregation is a persistent biomedical problem. Despite active research in disease-related aggregation, the need for multidisciplinary approaches to the problem is evident. Recent advances in single-molecule fluorescence spectroscopy are valuable for examining heterogenic biomolecular systems. In this work, we have explored the initial stages of amyloidogenic aggregation by employing fluorescence lifetime correlation spectroscopy (FLCS), an advanced modification of conventional fluorescence correlation spectroscopy (FCS) that utilizes time-resolved information. FLCS provides size distributions and kinetics for the oligomer growth of the SH3 domain of α-spectrin, whose N47A mutant forms amyloid fibrils at pH 3.2 and 37 °C in the presence of salt. The combination of FCS with additional fluorescence lifetime information provides an exciting approach to focus on the initial aggregation stages, allowing a better understanding of the fibrillization process, by providing multidimensional information, valuable in combination with other conventional methodologies.},
organization = {This work is funded by grant P10-FQM-6154 from the Consejeria de Innovacion, Ciencia y
Empresa (Junta de Andalucia).},
publisher = {MDPI},
keywords = {Amyloids},
keywords = {Protein aggregation},
keywords = {Pulsed interleaved excitation},
keywords = {Protein oligomers},
keywords = {Single-molecule fluorescence},
title = {Early Amyloidogenic Oligomerization Studied through Fluorescence Lifetime Correlation Spectroscopy},
doi = {10.3390/ijms13089400},
author = {Paredes, José M. and Casares Atienza, Salvador and Ruedas Rama, María José and Fernández, Elena and Castello, Fabio and Varela Álvarez, Lorena and Orte Gutiérrez, Ángel},
}