title: Interaction of chlorogenic acids and quinides from coffee with human serum albumin.
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.
authors.affiliation: 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.
authors.forename: Valentina
authors.initials: V
authors.lastname: Sinisi
authors.affiliation: Dipartimento di Scienze Chimiche e Farmaceutiche, Università degli Studi di Trieste, via L. Giorgieri 1, 34127 Trieste, Italy.
authors.forename: Cristina
authors.initials: C
authors.lastname: Forzato
authors.affiliation: Dipartimento di Scienze Chimiche e Farmaceutiche, Università degli Studi di Trieste, via L. Giorgieri 1, 34127 Trieste, Italy.
authors.forename: Nicola
authors.initials: N
authors.lastname: Cefarin
authors.affiliation: illycaffè S.p.A., via Flavia 110, 34147 Trieste, Italy.
authors.forename: Luciano
authors.initials: L
authors.lastname: Navarini
authors.affiliation: Dipartimento di Scienze Chimiche e Farmaceutiche, Università degli Studi di Trieste, via L. Giorgieri 1, 34127 Trieste, Italy. Electronic address: fberti@units.it.
authors.forename: Federico
authors.initials: F
authors.lastname: Berti
mesh_terms: D001665:Binding Sites; D002109:Caffeic Acids / Q000737:chemistry; D002726:Chlorogenic Acid / Q000031:analogs & derivatives / Q000737:chemistry; D003069:Coffee / Q000737:chemistry*; D003373:Coumaric Acids / Q000737:chemistry; D006801:Humans; D007783:Lactones / Q000737:chemistry; D059808:Polyphenols / Q000737:chemistry*; D011801:Quinic Acid / Q000031:analogs & derivatives / Q000737:chemistry; D012709:Serum Albumin / Q000737:chemistry*; D013050:Spectrometry, Fluorescence
chemical_list: D002109:Caffeic Acids; D002726:Chlorogenic Acid; D003069:Coffee; D003373:Coumaric Acids; D007783:Lactones; D059808:Polyphenols; D011801:Quinic Acid; D012709:Serum Albumin; C004999:ferulic acid; C473200:5-caffeoylquinic acid; C040048:caffeic acid
keywords: Chlorogenic acids; Coffee polyphenols; Fluorescence spectroscopy; Human serum albumin; Protein–ligand interaction