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Interaction of chlorogenic acids and quinides from coffee with human serum albumin.
Food Chem. 2015 Feb 01; 168:332-40.FC

Abstract

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.

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Publisher Full Text (DOI)

Authors+Show Affiliations

Sinisi V
Dipartimento di Scienze Chimiche e Farmaceutiche, Università degli Studi di Trieste, via L. Giorgieri 1, 34127 Trieste, Italy. Electronic address: valentina.sinisi@phd.units.it.
Forzato C
Dipartimento di Scienze Chimiche e Farmaceutiche, Università degli Studi di Trieste, via L. Giorgieri 1, 34127 Trieste, Italy.
Cefarin N
Dipartimento di Scienze Chimiche e Farmaceutiche, Università degli Studi di Trieste, via L. Giorgieri 1, 34127 Trieste, Italy.
Navarini L
illycaffè S.p.A., via Flavia 110, 34147 Trieste, Italy.
Berti F
Dipartimento di Scienze Chimiche e Farmaceutiche, Università degli Studi di Trieste, via L. Giorgieri 1, 34127 Trieste, Italy. Electronic address: fberti@units.it.

MeSH

Binding SitesCaffeic AcidsChlorogenic AcidCoffeeCoumaric AcidsHumansLactonesPolyphenolsQuinic AcidSerum AlbuminSpectrometry, Fluorescence

Pub Type(s)

Journal Article
Research Support, Non-U.S. Gov't

Language

eng

PubMed ID

25172718

Citation

Sinisi, Valentina, et al. "Interaction of Chlorogenic Acids and Quinides From Coffee With Human Serum Albumin." Food Chemistry, vol. 168, 2015, pp. 332-40.
Sinisi V, Forzato C, Cefarin N, et al. Interaction of chlorogenic acids and quinides from coffee with human serum albumin. Food Chem. 2015;168:332-40.
Sinisi, V., Forzato, C., Cefarin, N., Navarini, L., & Berti, F. (2015). Interaction of chlorogenic acids and quinides from coffee with human serum albumin. Food Chemistry, 168, 332-40. https://doi.org/10.1016/j.foodchem.2014.07.080
Sinisi V, et al. Interaction of Chlorogenic Acids and Quinides From Coffee With Human Serum Albumin. Food Chem. 2015 Feb 1;168:332-40. PubMed PMID: 25172718.
* Article titles in AMA citation format should be in sentence-case
TY - JOUR T1 - Interaction of chlorogenic acids and quinides from coffee with human serum albumin. AU - Sinisi,Valentina, AU - Forzato,Cristina, AU - Cefarin,Nicola, AU - Navarini,Luciano, AU - Berti,Federico, Y1 - 2014/07/24/ PY - 2014/02/10/received PY - 2014/06/11/revised PY - 2014/07/15/accepted PY - 2014/8/31/entrez PY - 2014/8/31/pubmed PY - 2015/12/15/medline KW - Chlorogenic acids KW - Coffee polyphenols KW - Fluorescence spectroscopy KW - Human serum albumin KW - Protein–ligand interaction SP - 332 EP - 40 JF - Food chemistry JO - Food Chem VL - 168 N2 - 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. SN - 1873-7072 UR - https://www.unboundmedicine.com/medline/citation/25172718/Interaction_of_chlorogenic_acids_and_quinides_from_coffee_with_human_serum_albumin_ DB - PRIME DP - Unbound Medicine ER -