Early Amyloidogenic Oligomerization Studied through Fluorescence Lifetime Correlation Spectroscopy Paredes, José M. Casares Atienza, Salvador Ruedas Rama, María José Fernández, Elena Castello, Fabio Varela Álvarez, Lorena Orte Gutiérrez, Ángel Amyloids Protein aggregation Pulsed interleaved excitation Protein oligomers Single-molecule fluorescence 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. 2013-10-22T10:30:26Z 2013-10-22T10:30:26Z 2012 info:eu-repo/semantics/article Paredes, J.M.; et al. Early Amyloidogenic Oligomerization Studied through Fluorescence Lifetime Correlation Spectroscopy. International Journal of Molecular Sciences, 13(8): 9400-9418 (2012). [http://hdl.handle.net/10481/28515] 1422-0067 http://hdl.handle.net/10481/28515 10.3390/ijms13089400 eng http://creativecommons.org/licenses/by-nc-nd/3.0/ info:eu-repo/semantics/openAccess Creative Commons Attribution-NonCommercial-NoDerivs 3.0 License MDPI