Insights on the Binding of Thioflavin Derivative Markers to Amyloid Fibril Models and Aβ_(1-40) Fibrilsfrom Computational Approaches

摘要

The present contribution analyzes the binding of ThT and neutral ThT derivatives to a 0-sheet model by means of quantum chemical calculations. In addition, we study the properties of four molecules: (2-(2-hydroxyphenyl)benzoxazole (HBX), 2-(2-hydroxyphenyl)benzothiazole (HBT) and their respective iodinated compounds, HBXI and HBTI, in binding to amyloid fibril models and Aβ_(1-40)fibrils by using a combination of docking, molecular dynamics and quantum mechanics calculations.