Binding mechanism and functional evaluation of quercetin 3-rhamnoside on lipase

Binding of the B-Raf Inhibitors Dabrafenib and Vemurafenib to Human Serum Albumin: A Biophysical and Molecular Simulation Study

“…The fluorescence quenching of aromatic amino acids is an efficient tool for determining the binding affinity and mechanism underlying ligand–protein interactions. − Indeed, when compared to alternative biophysical and biochemical methods for evaluating protein/ligand interaction, fluorescence quenching provides several advantages. , For instance, fluorescence intensity is directly proportional to the number of fluorophores present in a sample, which enables quantitative measurements. Also, fluorescence measurements have a very high sensitivity and may therefore be carried out on single molecules, allowing for the observation of biological mechanisms at the molecular level .…”

Investigation on the interaction between myricetin and dihydromyricetin with trypsin, α‐chymotrypsin, lysozyme by spectroscopy and molecular docking methods

“…In order to determine the acting force, one should determine the thermodynamic parameters, enthalpy change (Δ H ) and entropy change (Δ S ) of the reaction. The van't Hoff equation (Equation 4) and the Gibbs–Helmholtz equation (Equation 5) can be used to calculate the thermodynamic parameters [ 28,29 ] : …”

Blue honeysuckle extracts retarded starch digestion by inhibiting glycosidases and changing the starch structure

“…6D) at Δλ = 15 and 60 nm. The binding process had a greater impact on tryptophan because the fluorescence intensity decreased more obviously at Δλ = 60 nm than that at Δλ = 15 nm, 43 indicating that the site where BHE acts on the glycosidase was closer to tryptophan. Results indicated that BHE changed the microenvironment of the fluorophore around the active site of glycosidase, which might be one of the reasons for the decrease in enzyme activity.…”