Document Detail

Interaction of chlorogenic acids and quinides from coffee with human serum albumin.
MedLine Citation:
PMID:  25172718     Owner:  NLM     Status:  Publisher    
Chlorogenic acids and their derivatives are abundant in coffee and their composition changes between coffee species. Human serum albumin (HSA) interacts with this family of compounds with high affinity. We have studied by fluorescence spectroscopy the specific binding of HSA with eight compounds that belong to the coffee polyphenols family, four acids (caffeic acid, ferulic acid, 5-O-caffeoyl quinic acid, and 3,4-dimethoxycinnamic acid) and four lactones (3,4-O-dicaffeoyl-1,5-γ-quinide, 3-O-[3,4-(dimethoxy)cinnamoyl]-1,5-γ-quinide, 3,4-O-bis[3,4-(dimethoxy)cinnamoyl]-1,5-γ-quinide, and 1,3,4-O-tris[3,4-(dimethoxy)cinnamoyl]-1,5-γ-quinide), finding dissociation constants of the albumin-chlorogenic acids and albumin-quinides complexes in the micromolar range, between 2 and 30μM. Such values are comparable with those of the most powerful binders of albumin, and more favourable than the values obtained for the majority of drugs. Interestingly in the case of 3,4-O-dicaffeoyl-1,5-γ-quinide, we have observed the entrance of two ligand molecules in the same binding site, leading up to a first dissociation constant even in the hundred nanomolar range, which is to our knowledge the highest affinity ever observed for HSA and its ligands. The displacement of warfarin, a reference drug binding to HSA, by the quinide has also been demonstrated.
Valentina Sinisi; Cristina Forzato; Nicola Cefarin; Luciano Navarini; Federico Berti
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Publication Detail:
Type:  JOURNAL ARTICLE     Date:  2014-7-24
Journal Detail:
Title:  Food chemistry     Volume:  168C     ISSN:  0308-8146     ISO Abbreviation:  Food Chem     Publication Date:  2015 Feb 
Date Detail:
Created Date:  2014-8-30     Completed Date:  -     Revised Date:  -    
Medline Journal Info:
Nlm Unique ID:  7702639     Medline TA:  Food Chem     Country:  -    
Other Details:
Languages:  ENG     Pagination:  332-340     Citation Subset:  -    
Copyright Information:
Copyright © 2014 Elsevier Ltd. All rights reserved.
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