Role of catechin on collagen type I stability upon oxidation: a NMR approach |
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| Authors: | Massimo Lucarini Fabio Sciubba Donatella Capitani Maria Enrica Di Cocco Laura D’Evoli Alessandra Durazzo |
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| Institution: | 1. CREA – Research Centre for Food and Nutrition, Rome, Italy;2. massimo.lucarini@crea.gov.it;4. Department of Chemistry, “Sapienza” University of Rome, Rome, Italy;5. Magnetic Resonance Laboratory “Annalaura Segre”, Institute of Chemical Methodologies, National Research Council (CNR), Monterotondo (RM), Italy |
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| Abstract: | AbstractThe study focuses on the understanding, at molecular level, the mechanism of interaction between protein and flavonoids. Collagen and catechin interactions were investigated by NMR in solution and solid state. The effect of catechin on the stability of collagen to oxidation was also explored. Collagen was treated with two concentrations of catechin solutions. Oxidation was carried out by incubation of collagen solution with three oxidation systems: Fe(II)/H2O2, Cu(II)/H2O2, and NaOCl/H2O2. The effects of oxidation systems were evaluated by high resolution 1?D and 2?D proton spectroscopy and solid state NMR (13C CP MAS) experiments. Interactions between collagen and catechin preferentially occur between catechin B ring and the amino acids Pro and Hyp of collagen. Results showed that both iron and copper oxidation systems were able to interact with collagen by site specific attack. Moreover, catechin protects collagen proline from oxidation by metal/H2O2 systems, preventing copper and iron approach to collagene molecule;this behaviour was more evident for the copper/H2O2 system. |
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| Keywords: | Collagen Catechin CP-MAS NMR oxidation |
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