Binding mode of Thioflavin T in insulin amyloid fibrils

Deciphering metal-induced oxidative damages on glycated albumin structure and function

“…3c). The increasing interest on this molecule is revealed by several recent studies dealing on ThT-fibril interaction [42][43][44][45]. Emission fluorescence of ThT at 500 nm progressively increased in the presence of growing concentration of metal ions during albumin incubation with glucose.…”

Binding of streptomycin with bovine serum albumin: Energetics and conformational aspects

“…Though the interactions of some antibiotics with the serum albumin are reported in literature [11,[17][18][19], quantitative studies on the interaction of streptomycin with serum albumin addressing the energetics and type of interactions is not available in literature. A combination of isothermal titration calorimetry and fluorescence spectroscopy has yielded valuable information on binding interactions in biologically important systems both quantitatively and qualitatively [20][21][22][23][24][25]. In this work, we have used isothermal titration calorimetry in determining binding affinity, enthalpy, entropy and stoichometry …”

Binding Modes of Thioflavin T Molecules to Prion Peptide Assemblies Identified by Using Scanning Tunneling Microscopy

“…The central pore region of amyloid fibrils is one of the proposed binding locations determined by small-angle X-ray scattering and XRD. 18,19 The "channel" binding site formed by side chains of residues along the fibril axis have also been shown by many reports, which suggested the perpendicular orientation of the labeling molecular axes to the peptide strands. 11,21,22,24,25 The parallel orientation of probe molecules to the peptide strands is another proposed binding mode, which is paid more attention in the recently published theoretical studies.…”