A review on structure–affinity relationship of dietary flavonoids with serum albumins

Abstract

Flavonoids are a class of plant secondary metabolites and among thousands of flavonoids few are considered as dietary flavonoids. Serum albumin (SA), the most abundant protein in plasma, functions as the most important carrier of vital drugs, including dietary flavonoids. The binding affinity of dietary flavonoids to SA is demonstrated to be governed by structure-affinity relationship (SAR) and its bioavailability. The present review summarizes the interactions of flavonoids categorized as flavanol, flavonol, flavone, isoflavone, flavanones, and anthocyanidins with SAs (bovine serum albumin and human serum albumin) in light of SAR. The key findings are: (1) the position and degree of hydroxylation highly influence the affinity of flavonoids to SAs, (2) glycosylation decreases and substitution of methoxy group increases the affinity of flavonoids for SAs, (3) catechin gallates have higher binding affinity to SAs than catechins and gallocatechins, (4) inorganic metal ions modulate the binding affinity of flavonoids to SAs, and (5) hydrophobic interaction plays a major role in the interactions of all flavonoids with SAs.

Fluorescence spectroscopy and docking study in two flavonoids, isolated tectoridin and its aglycone tectorigenin, interacting with human serum albumin: a comparison study

“…The fairly large and highly polar flavonoid glycosides cannot be absorbed after oral ingestion, but are hydrolyzed to their aglycones by bacterial enzymes in vivo . This is supported by the metabolic process of TD shown previously , which proposes that TD is first hydrolyzed to TG, and TG shows more potent biological activity than TD.…”

“…Studies on the interaction mode of small molecules with HSA are quite important . The interaction between flavonoids and serum albumin has been well studied . Most reports have focused on the binding process between flavonoids and serum albumins; only a few have discussed the effect of flavonoid glycosylation on the characteristics of binding with protein .…”

Study on Structure Activity Relationship of Natural Flavonoids against Thrombin by Molecular Docking Virtual Screening Combined with Activity Evaluation In Vitro

“…These compounds elicit diverse pharmacological activity such as antioxidant, anti-inflammation, antibacterial, antithrombus and antineoplastic due to the difference in structural diversities in basic parent structure or substituent group [13]. Structure activity relationship (SAR) of flavonoids based on the above biological activities has gained lots of attention in recent years [14][15][16]. To the best of our knowledge, there is only one literature report on the SAR of flavonoids inhibiting thrombin [17].…”

Spectroscopic and molecular docking study on the structure–affinity relationship and mechanism in the interaction of genistein and its derivatives with bovine serum albumin

“…Another mechanism may be that the trifluoromethyl substitution at ring B at the 4′ position increased that molecular weight and hydrophobility, increased molecular weight can increase steric hindrance and weaken the capacity to penetrate into tryptophan‐rich hydrophobic regions of BSA. Increase in hydrophobicity and hydrophobic interaction plays a major role in the interactions of all flavonoids with SAs . We speculated the existence of a trifluoromethyl substitution at ring B at the 4′ position was secondary factor, because the binding affinity of GEN1 for BSA was higher than that for GEN, and the effect of steric hindrance and the effect of hydrophobic interaction were opposite.…”