Role of catechin on collagen type I stability upon oxidation: a NMR approach
| Autor: | Maurizio Delfini, Laura D'Evoli, Maria Enrica Di Cocco, Ginevra Lombardi Boccia, Donatella Capitani, Fabio Sciubba, Alessandra Durazzo, Massimo Lucarini |
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| Rok vydání: | 2020 |
| Předmět: |
Collagen type
Flavonoids Binding Sites Magnetic Resonance Spectroscopy 010405 organic chemistry Protein Stability Organic Chemistry food and beverages Proteins Catechin Plant Science Hydrogen Peroxide 01 natural sciences Biochemistry Collagen Type I 0104 chemical sciences Analytical Chemistry 010404 medicinal & biomolecular chemistry chemistry.chemical_compound Molecular level chemistry Metals Biophysics Oxidation-Reduction |
| DOI: | 10.6084/m9.figshare.7792082 |
| Popis: | The 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. |
| Databáze: | OpenAIRE |
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