Molecular structure-affinity relationship of dietary flavonoids for bovine serum albumin

Abstract

Abstract:The relationship between the molecular structure of dietary flavonoids and their affinities for bovine serum albumin (BSA) were fully investigated by fluorescence titration analysis. The binding process with BSA was significantly affected by the molecular structure of flavonoids under study. The methylation of hydroxyl group in flavonoids enhanced their binding affinities for BSA by 1 to 794 times. Hydroxylation on rings A, B and C also strongly influenced the affinity for BSA. The glycosylation weakened the affinities for BSA by 1-2 orders of magnitude depending on the conjugation site and the class of sugar moiety. The hydrogenation of the C2=C3 double bond slightly increased the binding affinity. The galloylated catechins and pyrogallol-type catechins exhibited higher binding affinities for BSA than non-galloylated and catecholtype catechins, respectively. The affinities for BSA increased with increasing partition coefficients and decreased with increasing hydrogen bond donor and acceptor numbers of flavonoids, which suggested that the binding interaction was mainly caused by hydrophobic forces.

Apigenin oxidovanadium(IV) cation interactions. Synthesis, spectral, bovine serum albumin binding, antioxidant and anticancer studies

“…Our results for K sv , K a , n and the thermodynamic parameters (negative values of DH and DS, see below) agree with previous data reported for apigenin [71]. On the other hand, it is important to mention that there are some discrepancies in the literature for the interaction of apigenin with bovine serum albumin being the K sv , K a or the thermodynamic parameters quite different from each other [72][73][74]. These differences have been attributed to the different experimental conditions used in each determination [74] (differences in albumin and flavonoid concentrations, albumin fractions and/or dissolution media: pH values and the concentrations of NaCl and Mg 2+ ).…”

Molecular Structure–Affinity Relationship of Flavonoids in Lotus Leaf (Nelumbo nucifera Gaertn.) on Binding to Human Serum Albumin and Bovine Serum Albumin by Spectroscopic Method

“…As shown in Table 2 , the calculated K q values of HSA and BSA fluorescence quenching by flavonoids were much higher than 2.0 × 10 10 L/mol/s (0.827 × 10 14 L/mol/s to 4.695 × 10 14 L/mol/s for HSA and 0.731 × 10 14 L/mol/s to 3.710 × 10 14 L/mol/s for BSA). It could be concluded that the fluorescence quenching of HSA and BSA by flavonoids was probably initiated by static quenching [ 31 ].…”

“…Considering the representative characteristics and the availability, the purified HSA and BSA are usually used as modeling proteins to investigate the interactions between small molecules and serum albumins. Binding of flavonoids to HSA was extensively studied using different fluorescence spectroscopy techniques [ 29 , 30 , 31 , 32 , 33 ]. The observed change in fluorescence enables the calculation of HSA-ligand complexes stability constants and also the distance between the ligand and Trp 214 [ 26 ].…”

The role of photo-electric properties of silk cocoon membrane in pupal metamorphosis: A natural solar cell

“…The 402 peak is possibly due to the presence of trace amount (0.05–0.10%) of a very closely related and structurally similar flavonoid viz. nobiletin, a fungi-static flavones present in most of the plants with -OCH3 substitutions, which co-elutes along with the major flavonol fraction of quercetin in the crude extract 25 26 27 28 29 .…”