6533b7d3fe1ef96bd1260592
RESEARCH PRODUCT
Phasor FLIM analysis of Thioflavin T fluorescence in protein amyloid aggregates: Mapping molecular interactions.
Giuseppe SancataldoDirk Fennema GalparsoroSara AnselmoMaurizio LeoneValeria Vetrisubject
FLIMprotein aggregateThioflavin Tphasor amyloidSettore FIS/07 - Fisica Applicata(Beni Culturali Ambientali Biol.e Medicin)description
Thioflavin T (ThT) is a worldwide used dye to monitor protein aggregation as it stains with a certain specificity amyloid structures. The interactions between ThT and its hosts are largely studied suggesting that fluorescence properties of this dye critically depend both on the environment rigidity, electrostatic and hydrophobic properties as well as on molecular details binding site structure. Here FLIM and phasor approach analysis are used to exploit ThT amyloid interactions and, in turn, to address polymorphism and structural heterogeneity of amyloid species mapping aggregate-to-aggregate structural differences and revealing details of molecular architecture within the same aggregate.
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