Abstract：
:The structural difference of flavonoids strongly affects the binding process with plasma proteins. This work in here mainly concerns about the molecular property-binding affinity relationship of dietary flavonoids for common rat plasma proteins (CRPP). The magnitudes of binding constants between flavonoids and CRPP were within the range of 10(4)-10(5) L/mol and the number of binding sites (n) was determined as 1.02 ± 0.19. These data were much smaller than the affinities between flavonoids and purified bovine and human serum albumins. The hydroxylation on rings A, B and C of flavonoids significantly affected the binding affinity. The glycosylation of dietary flavonoids decreased the binding affinity and the C2=C3 double bond hardly affected it. The galloylated catechins have higher binding affinities for CRPP than non-galloylated catechins. Flavonoids played as a hydrogen bond acceptor when bound to CRPP. The flavonoids with high topological polar surface areas (TPSA) are bound tightly while those with low TPSA are not.
journal_name
Biochimiejournal_title
Biochimieauthors
Xiao J,Cao H,Chen T,Yang F,Liu C,Xu Xdoi
10.1016/j.biochi.2010.08.013subject
Has Abstractpub_date
2011-02-01 00:00:00pages
134-40issue
2eissn
0300-9084issn
1638-6183pii
S0300-9084(10)00299-3journal_volume
93pub_type
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