Title : Thioflavin T is a fluorescent probe of the acetylcholinesterase peripheral site that reveals conformational interactions between the peripheral and acylation sites.

Pub. Date : 2001 Jun 29

PMID : 11313335






6 Functional Relationships(s)
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1 Thioflavin T is a fluorescent probe of the acetylcholinesterase peripheral site that reveals conformational interactions between the peripheral and acylation sites. thioflavin T acetylcholinesterase (Cartwright blood group) Homo sapiens
2 Here we report that thioflavin T, a fluorophore widely used to detect amyloid structure in proteins, binds selectively to the AChE peripheral site with an equilibrium dissociation constant of 1.0 microm. thioflavin T acetylcholinesterase (Cartwright blood group) Homo sapiens
3 The fluorescence of the bound thioflavin T is increased more than 1000-fold over that of unbound thioflavin T, the greatest enhancement of fluorescence for the binding of a fluorophore to AChE yet observed. thioflavin T acetylcholinesterase (Cartwright blood group) Homo sapiens
4 The fluorescence of the bound thioflavin T is increased more than 1000-fold over that of unbound thioflavin T, the greatest enhancement of fluorescence for the binding of a fluorophore to AChE yet observed. thioflavin T acetylcholinesterase (Cartwright blood group) Homo sapiens
5 The observation of this partial quenching of thioflavin T fluorescence is a major advance in the study of AChE for two reasons. thioflavin T acetylcholinesterase (Cartwright blood group) Homo sapiens
6 Second, it indicates that ligand binding to the acylation site initiates a change in the local AChE conformation at the peripheral site that quenches the fluorescence of bound thioflavin T. thioflavin T acetylcholinesterase (Cartwright blood group) Homo sapiens