Study on the interaction between promethazine hydrochloride and bovine serum albumin by fluorescence spectroscopy

Inhibitory kinetics and mechanism of kaempferol on α-glucosidase

“…In contrast, the maximum emission wavelength of Trp residue did not show any shift (Fig. 1D), indicating that the microenvironment around the Trp residue displayed no discernable change during the binding process (He et al, 2011).…”

Probing the binding interaction of human serum albumin with three bioactive constituents of Eriobotrta japonica leaves: Spectroscopic and molecular modeling approaches

“…3D fluorescence spectroscopy can provide detailed information on the conformational and microenvironmental changes of proteins that combine with small molecules [30]. The 3-D fluorescence spectral characteristics of the two systems of interest are listed in Table 4 in terms of peak position (k ex /k em ) and intensity [31,32].…”

Interaction Behavior Between Niclosamide and Pepsin Determined by Spectroscopic and Docking Methods

“…Generally, four representative interaction forces, namely, hydrophobic force, hydrogen bond interactions, van der Waals force, and electrostatic interactions, exist between small molecular substrates and biological macromolecules [33]. The aim of this subsection is to attempt to account for the symbols and magnitudes of the thermodynamic parameters of protein association reactions to analyze the molecular forces.…”