Induced and Inversed Circularly Polarized Luminescence of Achiral Thioflavin T Assembled on Peptide Fibril.

Chiroptical inversion of amyloid fibrils is a novel phenomenon and is of fundamental importance; however, the underlying structural basis remains poorly understood. Here, the co-assembly of Thioflavin T (ThT) with T1 amyloid fibril and the induced supramolecular chirality is investigated by induced circular dichroism (ICD) and circularly polarized luminescence (CPL), followed by direct morphological helicity observation of the fibril by an atomic force microscope (AFM). ThT exhibits negative ICD and CPL when assembled on the left-handed T1 fibril. Interestingly, when ThT dynamically interacts with the T1 fibril, the left-handed fibril partially converts into right-handed, accompanied with the inversion of CD and CPL signals. These results indicate that the morphological helicity of template fibril cannot be arbitrarily distinguished by the sign of chiroptical spectra of the dye/peptide assemblies.