Abstract

Computational modelling was used to construct the models of type I collagen and the Zr-Al-Ti complex, as well as simulating the interactions between them. Hydrogen bond and Van der Waalsʼ 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 TGdetections, 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.