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Last Updated: 3 years ago
supplement:
Quercetin
supplement:
Serum Albumin, Human
Research Papers that Mention the Interaction
“Moreover, both of the methylation on 3’ position of quercetin and the C2=C3 double bond of apigenin and quercetin decreased the affinities for HSA and BSA.”
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“The affinity of quercetin (3′, 4′) for HSA is about 100-times higher than that of kaempferol (4′).”
“The affinity for this site is large and we found that quercetin may effectively displace warfarin from HSA.”
“Consistently, HSA markedly increases the maximal concentration of a two-electron oxidation product of quercetin that is accumulated and then consumed in the course of the peroxidation.”
“The additional observation of the faster consumption of the single Trp residue in the presence of quercetin suggests that HSA enhances the antioxidant activity of quercetin by regenerating some of its oxidation products retaining a H-donating activity.”
“The steady-state emission data suggest that quercetin binds to two distinct sites in HSA from which the emissions from the normal tautomer and complex species take place.”
“Upon binding to human serum albumin HSA), quercetin undergoes dramatic enhancement in its fluorescence emission intensity, along with the appearance of dual emission behavior, consisting of normal and excited-state proton transfer (ESPT) fluorescence.”
“It was found that quercetin shows extrinsic optical activity on interaction with HSA.”
“Binding of quercetin with HSA leads to dramatic enhancement in the fluorescence emission intensity and anisotropy (r), along with significant changes in the fluorescence excitation and emission profiles.”
“The emission, excitation, and anisotropy (r=0.18 at [HSA]=30 microM) data (using the native …) along with emission studies of quercetin using partially denatured HSA (by 8M urea) indicate that the quercetin molecules bind at a motionally restricted site near …-214 in the interdomain cleft region of HSA.”
“Finally, quercetin was a good antioxidant in protecting lysozyme and beta-lactoglobulin A, but its binding to HSA resulted in a pro-oxidant effect that accelerated HSA fragmentation.”
Structural damage to proteins caused by free radicals: asessment, protection by antioxidants, and influence of protein binding.“When bound to domain IIA of HSA, quercetin repairs, by intra- or intermolecular encounter, less than 20% of oxidative damage to HSA.”
Mechanisms of flavonoid repair reactions with amino acid radicals in models of biological systems: a pulse radiolysis study in micelles and human serum albumin.“When bound to domain IIA of HSA, quercetin repairs, by intra- or intermolecular encounter, less than 20% of oxidative damage to HSA.”
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