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

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. Collag...

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Bibliographic Details
Published in:Natural product research 2020-01, Vol.34 (1), p.53-62
Main Authors: Lucarini, Massimo, Sciubba, Fabio, Capitani, Donatella, Di Cocco, Maria Enrica, D'Evoli, Laura, Durazzo, Alessandra, Delfini, Maurizio, Lombardi Boccia, Ginevra
Format: Article
Language:English
Subjects:
Amino acids
Binding Sites
Catechin
Catechin - chemistry
Catechin - metabolism
Catechin - pharmacology
Collagen
Collagen (type I)
Collagen Type I - chemistry
Collagen Type I - metabolism
Copper
CP-MAS NMR
Flavonoids
Flavonoids - chemistry
Flavonoids - metabolism
Hydrogen peroxide
Hydrogen Peroxide - chemistry
Iron
Magnetic Resonance Spectroscopy - methods
Metals - chemistry
NMR
Nuclear magnetic resonance
Oxidation
Oxidation-Reduction
Proline
Protein Stability - drug effects
Proteins - chemistry
Proteins - metabolism
Sodium hypochlorite
Solid state
Spectroscopy
Stability
Systems analysis
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Summary: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)/H 2 O 2 , Cu(II)/H 2 O 2 , and NaOCl/H 2 O 2 . 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/H 2 O 2 systems, preventing copper and iron approach to collagene molecule;this behaviour was more evident for the copper/H 2 O 2 system.
ISSN:1478-6419
1478-6427
DOI:10.1080/14786419.2019.1570509