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Prigent, S.V.E., Gruppen, H., Visser, A.J.W.G., van Koningsveld, G.A., de Jong, G.A.H. and Voragen, A.G.J. (2003) Effects of non-covalent interactions with 5-O- caffeoylquinic acid (chlorogenic acid) on the heat denaturation and solubility of globular proteins. Journal of Agricultural and Food Chemistry, 51(17), 5088-5095.

has been cited by the following article:

• TITLE: Binding of naturally occurring hydroxycinnamic acids to bovine serum albumin

  AUTHORS: Lucie Trnkova, Iva Bousova, Vladimir Kubicek, Jaroslav Drsata

  KEYWORDS: Bovine Serum Albumin; Hydroxycinnamic Acid; Fluorescence Quenching; Protein-Ligand Binding

  JOURNAL NAME: Natural Science, Vol.2 No.6, July 1, 2010

  ABSTRACT: Hydroxycinnamic acids (HCAs) possess numer- ous biological effects including antioxidant, antiallergic, antimicrobial, and immunomodulatory activities and due to these properties are widely used in folk medicine. Nevertheless, they can interact with protein molecules and cause some structural and functional changes. The possib- ility of HCAs binding to bovine serum albumin (BSA) under physiological conditions was inve- stigated by the UV-VIS absorption spectroscopy and fluorescence quenching method. Apart from rosmarinic acid, all tested HCAs quenched tryptophan fluorescence of BSA in the studied range of concentrations (0-20 μM) mainly by static quenching mechanism (formation of non- fluorescent HCA-BSA complexes). The binding constants, number of binding sites and free energy changes were determined. The binding affinities of HCAs were ranked in the order: chlorogenic acid > sinapic acid ≥ caffeic acid > ferulic acid > o-coumaric acid > p-coumaric acid ≥ m-coumaric acid, which was confirmed by spectral overlaps of BSA emission spectrum with absorption spectrum of HCA. All free energy changes possessed negative sign indicating the spontaneity of HCA-BSA interaction.