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

Stability of the Meat Protein Type I Collagen: Influence of pH, Ionic Strength, and Phenolic Antioxidant

“…NMR relaxometry also allowed to investigate the interaction between collagen and catechin, an antioxidant molecule used in meat processing. In a previous work [7], it has been shown, from mono- Catechin strongly affects the T 22 and T 23 water relaxation times of collagen. As mentioned before, the intermediate T 22 was attributed to the water fraction in the interfibrillar space, and the third fraction (T 23 ) corresponded to the free water fraction.…”

“…NMR relaxometry also allowed to investigate the interaction between collagen and catechin, an antioxidant molecule used in meat processing. In a previous work [7], it has been shown, from monoand bi-dimensional proton NMR and 13 C cross polarization magic angle spectroscopy experiments, that collagen-catechin interactions preferentially occur between the catechin B ring and the collagen proline and hydroxyproline amino acids. The results reported in this study can give further information on the interaction between catechin and collagen, indicating that catechin is able to bind collagen both on the fibrillar surface and inside the interfibrillar spaces of the polymer, giving a deeper insight in the understanding of the interaction between catechin and collagen.…”

“…Collagen (2.5 mg/mL) was treated with catechin (0.001 M) for 24 h at room temperature (25 • C) in the dark and without any shaking, as described in the supplementary material of a previously published work by Lucarini et al [7]. Catechin solutions were spectrophotometrically titrated at 280 nm using a Cary 60 UV-Vis spectrophotometer (Agilent Technologies, Santa Clara, CA, USA) before and after the collagen addition to estimate the catechin amount in the complex.…”

“…Recently, a mechanism for the antioxidant action of catechin, a flavan-3-ol, namely (2R, 3S)-2-(3,4-dihydroxyphenyl)-3,4-dihydro-2H-chromene-3,5,7-triol, towards collagen, has been proposed [7]. Madhan et al [8], by using circular dichroism and Fourier transform infrared spectroscopy (FTIR), reported how hydrogen bonding and hydrophobic interactions represent the main forces in collagen stabilization due to the interaction with vegetal origin polyphenols.…”

In Vitro Characterization, Modelling, and Antioxidant Properties of Polyphenon-60 from Green Tea in Eudragit S100-2 Chitosan Microspheres

“…From a quick search using as keywords "epigallocatechin and nanoparticles" 376 publications appeared indexed in the Web of Science dated between 2000 and 2020, while "green tea and nanoparticles" resulted in the list of 780 publications. When associating epigallocatechin and dyslipidemia/dyslipidemia [13], only 33 works were listed as published over the last 20 years. While the molecular mechanisms involved in the effect of catechins on the metabolism of lipids and sugars remains to be fully described, catechins are known to induce antioxidant enzymes, inhibit pro-oxidant enzymes and scavenge reactive oxygen species (ROS), and to chelate metals [14][15][16]. EGCG has been reported to improve insulin-resistance and metabolic profiles, as well as to reduce adipocyte area as a consequence of lipolytic action [17].…”