Residue-Specific Binding Mechanisms of Thioflavin T to a Surface of Flat β-Sheets within a Peptide Self-Assembly Mimic
Sae Namioka, Norio Yoshida, Hiroyuki Konno, Koki Makabe
Abstract
) is important for binding of ThT. Positive charges introduced by histidine under a low-pH condition at the channel repel the binding of cationic ThT. Furthermore, we found a positive to negative conversion in the vicinity of the binding channel increases ThT fluorescence 4-fold. A detailed understanding of the ThT binding mechanism will enhance our ability to develop amyloid-specific small molecules.
Topics & Concepts
ThioflavinChemistryHistidineTyrosineDissociation constantPeptideBiophysicsFluorescenceMutantResidue (chemistry)Binding siteStereochemistryFluorescence anisotropyBiochemistryEnzymeReceptorBiologyAlzheimer's diseasePhysicsGenePathologyQuantum mechanicsMedicineMembraneDiseaseAlzheimer's disease research and treatmentsSupramolecular Self-Assembly in MaterialsProtein Structure and Dynamics