title: Thioflavin T forms a non-fluorescent complex with α-helical poly-L-glutamic acid.
abstract: Thioflavin T (ThT) is a molecular-rotor-type fluorophore reputed for the selective binding to amyloid fibrils. Using induced circular dichroism, here we show that ThT binds in an orderly manner to α-helical poly-L-glutamic acid (PLGA) implying that neither stacked β-sheets nor π-π stacking interactions are necessary for the binding between the dye and proteins.
authors: Department of Chemistry, University of Warsaw, Pasteura 1, 02-093 Warsaw, Poland.
authors: Viktoria
authors: V
authors: Babenko
authors: Wojciech
authors: W
authors: Dzwolak
mesh_terms: D000682:Amyloid / Q000737:chemistry; D052160:Benzothiazoles; D002942:Circular Dichroism; D006863:Hydrogen-Ion Concentration; D011099:Polyglutamic Acid / Q000737:chemistry*; D017433:Protein Structure, Secondary; D013053:Spectrophotometry; D013696:Temperature; D013844:Thiazoles / Q000737:chemistry*
chemical_list: D000682:Amyloid; D052160:Benzothiazoles; D013844:Thiazoles; C009462:thioflavin T; D011099:Polyglutamic Acid