Effect of Zinc (II) on the interactions of bovine serum albumin with flavonols bearing different number of hydroxyl substituent on B-ring

Effect of Cu2+ and Fe3+ for drug delivery: Decreased binding affinity of ilaprazole to bovine serum albumin

“…Metal ions or their complex can react with serum albumins [16][17][18][19][20], which then can affect the reactions of the drugs and serum albumin. The interactions between serum albumin and a few kinds of drugs, such as flavonoids [21][22][23], vitamins [24] and dexamethasone [25] in the presence of metal ions have been reported. The results indicated that the presence of metal ions could change the binding constants between drugs and BSA.…”

Structure-affinity relationship of bovine serum albumin with dietary flavonoids with different C-ring substituents in the presence of Fe3+ ion

“…Moreover, it has been found that metal-flavonoid complexes are redox active and play a meaningful role in the antioxidant, anticancer, anti-inflammatory, and antibacterial properties, which are often more active than the free flavonoids (Kostyuk, Potapovich, Strigunova, Kostyuk, & Afanasév, 2004;Ni, Du, & Kobot, 2007;Teixeira et al, 2005). The interactions between serum albumin and a few kinds of ligands, such as flavonoids (Cao, Jiang, & Chen, 2010;Li, Zhu, Xu, Chen, & Li, 2011;, vitamins (Shaikh, Seetharamappa, Kandagal, & Manjunatha, 2007) and dexamethasone (Naik, Chimatadar, & Nandibewoor, 2010) in the presence of metal ions have thus been reported. The results indicated that the presence of metal ions could change the binding constants between ligands and serum albumin.…”

Myricetin: A Naturally Occurring Regulator of Metal‐Induced Amyloid‐β Aggregation and Neurotoxicity

“…[15][16][17][18][19][20][21][22] These naturally occurring compounds have been shown independently to chelate metal ions and to interact with Ab, suggesting their potential bifunctionality toward metal-Ab species. [19][20][21][22][23][24][25] One of the flavonoid compounds, myricetin (Scheme 1), previously demonstrated an anti-amyloidogenic effect through its reversible binding to fibrillar Ab but not to the monomeric species. [21] In the case of its metal binding property, prior stud-ies have shown that myricetin has multiple potential sites for metal chelation including positions between the 4-oxo and the 3-or 5-OH groups (Scheme 1) that can form complexes with a binding stoichiometry of 1:1 or 1:2, metal/myricetin.…”