Entropy‐driven binding of octyl gallate in albumin: Failure in the application of temperature effect to distinguish dynamic and static fluorescence quenching

Abstract

Fluorescence quenching is widely used to obtain association constants between proteins and ligands. This methodology is based on assumption that ground-state complex between protein and ligand is responsible for quenching. Here, we call the attention about the risk of using the temperature criterion for decision of applying or not fluorescence quenching data to measure association constants. We demonstrated that hydrophobic effect can be the major force involved in the interaction and, as such, superposes the well-established rationalization that host/guest com-

Plant-inspired Pluronic–gallol micelles with low critical micelle concentration, high colloidal stability, and protein affinity

“…33 In addition to that, previous studies have demonstrated that the gallol moiety of octyl gallate blocks the enzyme activity of α-amylase, squalene epoxidase, and lipoxygenase by non-specific binding to their active site. 34–39 Thus, the enzymatic resistance of Plu–GA micelles could help protect encapsulated hydrophobic drugs.…”