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Natural Product Research
Formerly Natural Product Letters
Volume 34, 2020 - Issue 1: Ethnomedicine and Foods sources: novel perspectives. Guest Editor: Nicola Cicero
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Research Articles

Role of catechin on collagen type I stability upon oxidation: a NMR approach

Massimo LucariniCREA – Research Centre for Food and Nutrition, Rome, Italy; Correspondence[email protected]
ORCID Iconhttp://orcid.org/0000-0001-6178-9779
ORCID Icon,
Fabio SciubbaDepartment of Chemistry, “Sapienza” University of Rome, Rome, Italy; ORCID Iconhttp://orcid.org/0000-0002-1982-2712
ORCID Icon,
Donatella CapitaniMagnetic Resonance Laboratory “Annalaura Segre”, Institute of Chemical Methodologies, National Research Council (CNR), Monterotondo (RM), ItalyORCID Iconhttp://orcid.org/0000-0003-2392-0187
ORCID Icon,
Maria Enrica Di CoccoDepartment of Chemistry, “Sapienza” University of Rome, Rome, Italy; ORCID Iconhttp://orcid.org/0000-0003-4262-9360
ORCID Icon,
Laura D’EvoliCREA – Research Centre for Food and Nutrition, Rome, Italy;
,
Alessandra DurazzoCREA – Research Centre for Food and Nutrition, Rome, Italy; ORCID Iconhttp://orcid.org/0000-0002-7747-9107
ORCID Icon,
Maurizio DelfiniDepartment of Chemistry, “Sapienza” University of Rome, Rome, Italy; ORCID Iconhttp://orcid.org/0000-0002-6317-2024
ORCID Icon &
Ginevra Lombardi BocciaCREA – Research Centre for Food and Nutrition, Rome, Italy; ORCID Iconhttp://orcid.org/0000-0002-0944-2679
ORCID Icon show all
Pages 53-62 | Received 20 Nov 2018, Accepted 08 Jan 2019, Published online: 01 Mar 2019
 
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Abstract

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.

Disclosure statement

No potential conflict of interest was reported by the authors.

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