| Titre : |
Quantitative and structural analysis of isotopically labelled natural crosslinks in type I skin collagen using LC-HRMS and SANS |
| Type de document : |
texte imprimé |
| Auteurs : |
Yi Zhang, Auteur ; Rafea Naffa, Auteur ; Christopher J. Garvey, Auteur ; Catherine Maidment, Auteur ; Sujay Prabakar, Auteur |
| Année de publication : |
2019 |
| Article en page(s) : |
9 p. |
| Note générale : |
Bibliogr. |
| Langues : |
Anglais (eng) |
| Catégories : |
Analyse quantitative (chimie)
Chromatographie en phase liquide
Collagène -- Structure
Cuirs et peaux
Réticulation (polymérisation)
Spectrométrie de masse
Traceurs radioactifs
|
| Index. décimale : |
675 Technologie du cuir et de la fourrure |
| Résumé : |
Collagen structure in biological tissues imparts its intrinsic physical properties by the formation of several covalent crosslinks. For the first time, two major crosslinks in the skin dihydroxylysinonorleucine (HLNL) and histidinohydroxymerodesmosine (HHMD), were isotopically labelled and then analysed by liquid-chromatography high-resolution accurate-mass mass spectrometry (LC-HRMS) and small-angle neutron scattering (SANS). The isotopic labelling followed by LC-HRMS confirmed the presence of one imino group in both HLNL and HHMD, making them more susceptible to degrade at low pH. The structural changes in collagen due to extreme changes in the pH and chrome tanning were highlighted by the SANS contrast variation between isotopic labelled and unlabelled crosslinks. This provided a better understanding of the interaction of natural crosslinks with the chromium sulphate in collagen suggesting that the development of a benign crosslinking method can help retain the intrinsic physical properties of the leather. This analytical method can also be applied to study artificial crosslinking in other collagenous tissues for biomedical applications. |
| Note de contenu : |
- EXPERIMENTAL METHODS : Materials and methods
- RESULTS AND DISCUSSION : Characterization of natural crosslinks in skin collagen : isotopic labelling using NaBD4 and mechanism of HHMD formation - Quantification of natural crosslinks in skin collagen : relationship with pH and crosslinking conditions - Structural analysis of skin collagen : interplay between natural and artificial crosslinks
- Table 1 : Collagen D-periodicity at different processing stages in control, reduced and labelled skin samples. The D-period decreased for all samples starting from raw to the pickled stage, then increased at the crosslinked stage |
| DOI : |
https://doi.org/10.1186/s42825-019-0012-x |
| En ligne : |
https://link.springer.com/content/pdf/10.1186/s42825-019-0012-x.pdf |
| Format de la ressource électronique : |
Pdf |
| Permalink : |
https://e-campus.itech.fr/pmb/opac_css/index.php?lvl=notice_display&id=36955 |
in JOURNAL OF LEATHER SCIENCE AND ENGINEERING > Vol. 1 (Année 2019) . - 9 p.
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Quantitative and structural analysis of isotopically labelled natural crosslinks in type I skin collagen using LC-HRMS and SANS in JOURNAL OF LEATHER SCIENCE AND ENGINEERING, Vol. 1 (Année 2019)
