Journal
CHEMICAL COMMUNICATIONS
Volume 47, Issue 38, Pages 10686-10688Publisher
ROYAL SOC CHEMISTRY
DOI: 10.1039/c1cc14230e
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- Polish Ministry of Education and Science [NN 301 101236]
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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 alpha-helical poly-L-glutamic acid (PLGA) implying that neither stacked beta-sheets nor pi-pi stacking interactions are necessary for the binding between the dye and proteins.
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