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dc.contributor.authorParedes, José M.
dc.contributor.authorCasares Atienza, Salvador 
dc.contributor.authorRuedas Rama, María José 
dc.contributor.authorFernández, Elena
dc.contributor.authorCastello, Fabio
dc.contributor.authorVarela Álvarez, Lorena
dc.contributor.authorOrte Gutiérrez, Ángel 
dc.date.accessioned2013-10-22T10:30:26Z
dc.date.available2013-10-22T10:30:26Z
dc.date.issued2012
dc.identifier.citationParedes, 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]es_ES
dc.identifier.issn1422-0067
dc.identifier.urihttp://hdl.handle.net/10481/28515
dc.description.abstractAmyloidogenic 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.es_ES
dc.description.sponsorshipThis work is funded by grant P10-FQM-6154 from the Consejeria de Innovacion, Ciencia y Empresa (Junta de Andalucia).es_ES
dc.language.isoenges_ES
dc.publisherMDPIes_ES
dc.rightsCreative Commons Attribution-NonCommercial-NoDerivs 3.0 Licensees_ES
dc.rights.urihttp://creativecommons.org/licenses/by-nc-nd/3.0/es_ES
dc.subjectAmyloidses_ES
dc.subjectProtein aggregationes_ES
dc.subjectPulsed interleaved excitationes_ES
dc.subjectProtein oligomerses_ES
dc.subjectSingle-molecule fluorescencees_ES
dc.titleEarly Amyloidogenic Oligomerization Studied through Fluorescence Lifetime Correlation Spectroscopyes_ES
dc.typeinfo:eu-repo/semantics/articlees_ES
dc.rights.accessRightsinfo:eu-repo/semantics/openAccesses_ES
dc.identifier.doi10.3390/ijms13089400es_ES


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