Role of catechin on collagen type I stability upon oxidation: a NMR approach. Issue 1 (2nd January 2020)

• Record Type: Journal Article
• Authors: Lucarini, Massimo; Sciubba, Fabio; Capitani, Donatella; Di Cocco, Maria Enrica; D'Evoli, Laura; Durazzo, Alessandra; Delfini, Maurizio; Lombardi Boccia, Ginevra
• Is Part Of: Natural product research. Volume 34:Issue 1(2020)
• Page Start: 53
• Page End: 62
• Publication Date: 2020-01-02
• Subjects: Collagen -- Catechin -- CP-MAS NMR -- oxidation; Natural products -- Periodicals; Natural products -- Research -- Periodicals; Biological Factors -- Periodicals; Biological Products -- Periodicals; 547
• DOI: 10.1080/14786419.2019.1570509
• Languages: English
• ISSNs: 1478-6419

Abstract

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)/H2 O2, Cu(II)/H2 O2, and NaOCl/H2 O2 . The effects of oxidation systems were evaluated by high resolution 1 D and 2 D proton spectroscopy and solid state NMR ( 13 C 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/H2 O2 systems, preventing copper and iron approach to collagene molecule;this behaviour was more evident for the copper/H2 O2 system. Abstract :