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A Review of Dietary Polyphenol-Plasma Protein Interactions: Characterization, Influence on the Bioactivity, and Structure-Affinity Relationship
JIANBO XIAO; GUOYIN KAI
2012
Source PublicationCritical reviews in food science and nutrition
ISSN1040-8398
Volume52Issue:1-3Pages:85-101
Abstract


 

Other Abstract

The interactions between polyphenols, especially flavonoids and plasma proteins, have attracted great interest among researchers. Few papers, however, have focused on the structure-affinity relationship of polyphenols on their affinities for plasma proteins. The aim of this review is to give an overview of the research reports on the characterization, influence on the bioactivity, and the structure-affinity relationship for studying the affinities between polyphenols and plasma proteins. The molecular properties that influence the affinities of polyphenols for plasma proteins are the following: 1) One or more hydroxyl groups in the B-ring (e.g., 3,4 dihydroxylated B ring catechol group) of flavonoids enhanced the binding affinities toproteins.However,thehydroxylgroupintheC-ringwillweakenthebindinginteraction.2)Thepresenceofanunsaturated 2,3-bond in conjugation with a 4-carbonyl group, characteristic of flavonols structure, has been associated with stronger binding affinity with plasma proteins; 3) The glycosylation of flavonoids decreases the affinities for plasma proteins by 1–3 orders of magnitude depending on the conjugation site and the class of sugar moiety; 4) The methylation of hydroxyl groups in flavonoids slightly enhanced the affinities for plasma proteins by 2–16 times; 5) The galloylated catechins have higherbindingaffinitiesforplasmaproteinsthandonon-galloylatedcatechinsandthepyrogallol-typecatechinshavehigher affinities than do the catechol-type catechins. The affinity of the catechin with 2,3-trans structure was lower than those of the catechin with 2,3-cis structure; 6) The gallotannins with more gallol groups presented a much higher percentage of binding to plasma proteins. α-D-Gallotannin showed a greater affinity for plasma proteins than does the natural stereoisomer, β-D-gallotannin;7)Thebindingdegreeofchlorogenicacidwithonlyonecaffeoylgroupwaslowerthanthebindingdegrees of caffeoyl quinic acids with more caffeoyl groups. The methylation of phenolic acid decreased the affinity for BSA.

KeywordPolyphenols Plasma Proteins Structure-affinity Relationship Characterization
DOIhttps://doi.org/10.1080/10408398.2010.499017
Indexed BySCI
Language英语
WOS Research AreaFood Science & Technology ; Nutrition & Dietetics
WOS SubjectFood Science & Technology ; Nutrition & Dietetics
WOS IDWOS:000299917100007
PublisherTAYLOR & FRANCIS INC, 325 CHESTNUT ST, SUITE 800, PHILADELPHIA, PA 19106 USA
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Cited Times [WOS]:128   [WOS Record]     [Related Records in WOS]
Document TypeJournal article
CollectionInstitute of Chinese Medical Sciences
Corresponding AuthorJIANBO XIAO
AffiliationCollege of Life & Environment Science, Shanghai Normal University, Shanghai, PR China
Recommended Citation
GB/T 7714
JIANBO XIAO,GUOYIN KAI. A Review of Dietary Polyphenol-Plasma Protein Interactions: Characterization, Influence on the Bioactivity, and Structure-Affinity Relationship[J]. Critical reviews in food science and nutrition,2012,52(1-3):85-101.
APA JIANBO XIAO,&GUOYIN KAI.(2012).A Review of Dietary Polyphenol-Plasma Protein Interactions: Characterization, Influence on the Bioactivity, and Structure-Affinity Relationship.Critical reviews in food science and nutrition,52(1-3),85-101.
MLA JIANBO XIAO,et al."A Review of Dietary Polyphenol-Plasma Protein Interactions: Characterization, Influence on the Bioactivity, and Structure-Affinity Relationship".Critical reviews in food science and nutrition 52.1-3(2012):85-101.
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