New advances in the study on the interaction of [Cr(phen)2(dppz)]3+ complex with biological models; association to transporting proteins

Binding of [Cr(phen)3]3+ to transferrin at extracellular and endosomal pHs: Potential application in photodynamic therapy

“…However, the electrostatic interaction cannot be excluded in view of the charges of the species involved. These results reveal that the [Cr(phen) 3 ] 3+ stabilizes holoTf with a strong entropic contribution as was found for the process of binding between [Cr(phen) 3 ] 3+ and apoTf [22] and [Cr(phen) 3 ] 3+ and albumin [33].…”

“…), with increasing concentrations of Cr(III) complex according to the Bhattacharyya model (Eq. (3)) [32,33]:…”

“…This result indicates that both mechanisms (static and dynamic) of quenching can take place in the protein association process. This behavior has been described in processes of binding between Cr(III) complexes with apoTf and albumins [22,33]. This type of deviation occurs when quencher molecules interact with tryptophan and tyrosine residues causing the fluorescence quenching; then they change their position within the fluorophore microenvironment making room for the other molecules of the quencher.…”

A mononuclear Cu(II) complex with 5,6-diphenyl-3-(2-pyridyl)-1,2,4-triazine: Synthesis, crystal structure, DNA- and BSA-binding, molecular modeling, and anticancer activity against MCF-7, A-549, and HT-29 cell lines

“…At λ ex = 280 nm, the magnitude of the binding constants increases with increasing the temperature, which is due to increase in the stability of the BSA-complex system and shows that the binding process is endothermic. At λ ex = 295 nm, the magnitude of the binding constants decreases with increasing the temperature, which is due to decrease in the stability of the BSA-complex system and shows that the binding process is exothermic [67]. All of the binding constants are large and indicate that the interaction between BSA and the Cu(II) complex is very strong.…”

“…9-11) and using κ 2 = 2/3, η = 1.336, and Ф = 0.15 [73], the following parameters were calculated: J = 9.35 × 10 -13 cm 3 L mol -1 , R 0 = 5.37 nm, E = 0.55, and r = 5.19 nm. The donor-to-acceptor distance (r) is smaller than 10 nm [67], indicating that the energy transfer from BSA to the Cu(II) complex occurs with high probability.…”