In vitro tyrosinase, acetylcholinesterase, and HSA evaluation of dioxidovanadium (V) complexes: An experimental and theoretical approach

Vanadium(v) complexes derived from triphenylphosphonium and hydrazides: cytotoxicity evaluation and interaction with biomolecules

“…56 The enolate form of hydrazone ligands coordinated to dioxidovanadium( v ) is common in the literature. 57–59…”

“…48,71,72 All binding sites are able to accommodate the vanadium( v ) complexes, however, site III is the main pocket according to the molecular docking score values (Table 4). Reported in silico data indicated site I or site III as the main binding pockets for the interaction between HSA and some V V -complexes derived from pyridoxal or salicylaldehyde, 31,57 suggesting a dependence on the nature of the ligands in the interactive profile with albumin.…”

Spectroscopic studies and molecular docking on the interaction of delphinidin‐3‐O‐galactoside with tyrosinase

“…The two negative bands differed between free TY and the DG–TY complex, which was indicative of the loss of α‐helical structure. The percentage of protein α‐helix structure decreased, indicating that the DG bound to the amino acid residue of the main polypeptide chain of the TY protein and destroyed their hydrogen bonding networks 61 . Meanwhile, the CD spectra of TY protein in both TY and DG–TY system were similar in shape, indicating that the TY structure was major α‐helical after binding with DG 62,63 .…”

“…The percentage of protein α-helix structure decreased, indicating that the DG bound to the amino acid residue of the main polypeptide chain [TY] = 2.5 × 10 −7 mol L −1 , the mole ratio of DG/TY system were 0:1, 3:1, and 6:1 for curves a, b, and c, respectively of the TY protein and destroyed their hydrogen bonding networks. 61 Meanwhile, the CD spectra of TY protein in both TY and DG-TY system were similar in shape, indicating that the TY structure was major α-helical after binding with DG. 62,63 In a conclusion, some conformational changes of TY protein were observed after binding with DG.…”

Bromo‐Substituted Diazenyl‐pyrazolo[1,5‐a]pyrimidin‐2‐amines: Sonogashira Cross‐Coupling Reaction, Photophysical Properties, Bio‐interaction and HSA Light‐Up Sensor

“…Since derivatives showed significant absorption at the excitation wavelengths used for HSA binding studies, the inner filter correction was applied to the steady-state fluorescence data according to the literature. [46,47] Upon the inner filter correction in the fluorescence data to obtain quantitative information on the binding affinity of the interaction between HSA and derivatives studied here, the modified Stern-Volmer Equation (4) were applied, in which, F 0 and F are the steady-state fluorescence intensities of HSA in the absence and presence of compounds, respectively. The [Q], K SV , and k q are the derivative concentration, Stern-Volmer quenching constant, and bimolecular quenching rate constant, respectively.…”