Protein interactions with cyanidin‐3‐glucoside and its influence on α‐amylase activity |
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| Authors: | Stefanie Wiese Sonja Gärtner Harshadrai M Rawel Peter Winterhalter Sabine E Kulling |
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| Affiliation: | 1. University of Potsdam, Institute of Nutritional Science, Food Chemistry, D‐14558 Nuthetal, A.‐Scheunert Allee 114‐116, Germany;2. Technical University of Braunschweig, Institute of Food Chemistry, Schleinitzstrasse 20, 38106 Braunschweig, Germany |
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| Abstract: | BACKGROUND: Recent studies indicate that the bioavailability of anthocyanins is extremely low. One of the possible reasons could be their binding to proteins. Therefore, the binding affinity of cyanidin‐3‐glucoside (Cy3glc) to HSA and α‐amylase was investigated by the quenching of protein tryptophan fluorescence. From data obtained, the binding constants and the free Gibbs energy were calculated. The changes in conformation of the proteins tested were studied with circular dichroism and the influence of binding on α‐amylase activity determined. RESULTS: Cy3glc quenched the tryptophan fluorescence and upon ligand binding a change in protein structure was observed related to the corresponding decrease in the α‐amylase activity. The association constants of 25 to 77 × 103 L mol?1 were calculated for different proteins, indicating weak interactions of non‐covalent nature. Competitive binding with HSA in the presence of 8‐anilino‐1‐naphthalene sulfonic acid suggest involvement of hydrophobic interactions, in the case of HSA the possible site being subdomain IIA. CONCLUSION: The strongest affinity of Cy3glc for HSA being at pH 7 underlines its potential in transport and distribution of the phenolic compounds in organisms. An influence on salivary amylase activity is possible when drinking berry juices with high anthocyanins content. Copyright © 2008 Society of Chemical Industry |
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| Keywords: | protein– phenol interactions amylase activity anthocyanins cyanidin‐3‐glucoside tryptophan quenching circular dichroism |
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