Molecular interactions between type I collagen and metal complex : from computational modelling to experimental characterisation / Xiao Shiwei in JOURNAL OF THE SOCIETY OF LEATHER TECHNOLOGISTS & CHEMISTS (JSLTC), Vol. 102, N° 4 (07-08/2018)  

[article]  inJOURNAL OF THE SOCIETY OF LEATHER TECHNOLOGISTS & CHEMISTS (JSLTC) > Vol. 102, N° 4 (07-08/2018) . - p. 174-180 Titre : Molecular interactions between type I collagen and metal complex : from computational modelling to experimental characterisation Type de document : texte imprimé Auteurs : Xiao Shiwei, Auteur ; Dan Nianhua, Auteur ; Wang Kangjian ; Juxia Gong ; Dan Weihua ; Hong Lin Année de publication : 2018 Article en page(s) : p. 174-180 Note générale : Bibliogr. Langues : Anglais (eng) Catégories : Analyse spectrale Analyse thermique Caractérisation Collagène Complexes métalliques Dynamique moléculaire Microscopie Modèles numériques Morphologie (matériaux) Stabilité thermique Thermogravimétrie Index. décimale : 675 Technologie du cuir et de la fourrure Résumé : Computational modelling was used to construct the models of type I collagen and the Zr-AI-Ti complex, as well as simulating the interactions between them. Hydrogen bond and Van der Waals' forces exist between collagen and the Zr-Al-Ti complex. Furthermore, other bonding regions between central metal ions and O, N, H atoms were calculated. Furthermore, experimental characterisations were carried out to better verify the results of computational modelling, results showed that the spectra of FTIR, UV-DRS and fluorescence were all shifted to some extent. Specifically, UV-DRS and fluorescence detection suggested that the alteration appeared around aromatic residues, tyrosine and phenylalanine. Further, XPS proved that the N atom showed a higher possibility of coordinating with the metal complex than did O. Accompanied with DSC and TG detections, it has been confirmed that the interactions brought by Zr-Al-Ti complex gave rise to the increase of denaturation temperature of collagen from 66.51°C to 88.1°C. In addition, results obtained from SEM and AFM show It is obvious that the original collagen fibre has been changed into a tight layer by layer structure, and it could be observed that metal complex particles filled in between collagen fibres ,this together with strong chemical bonding between them, finally stabilized the structure of collagen. Note de contenu : - EXPERIMENTAL PROCEDURES : Reagents and chemicals - Computational modeling - Optimisation of reaction between collagen and Zr-Al-Ti complex - Free amino content - Free carboxyl content - Fourrier transformed intrared spectroscoy (FTIR) - Diffused reflectance spectrum (UV-DRS) - Fluorescence spectrum - X-ray photoelectron spectroscopy (XPS) - Differential scanning calorimetry (DSC) and thermogravimetry (TG) - Scanninc electron microscopy (SEM) - Atomic force microscopy (AFM) - RESULTS AND DISCUSSION : Computational modeling - Modification degree - Spectrum analysis - XPS analysis - Thermal stability - Morphology En ligne : https://drive.google.com/file/d/1o3e0lqalQCBbpE3iChLxMEBDI0WVh_Oz/view?usp=drive [...] Format de la ressource électronique : Pdf Permalink : https://e-campus.itech.fr/pmb/opac_css/index.php?lvl=notice_display&id=30899 [article]

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