A comparative study on cross-linking of fibrillar gel prepared by tilapia collagen and hyaluronic acid with EDC/NHS and genipin

An antibacterial and healing-promoting collagen fibril constructed by the simultaneous strategy of fibril reconstitution and ε-polylysine anchoring for infected wound repair

“…2b), the peaks with binding energies near 284.8 eV, 286.2 eV, and 288.0 eV correspond to the saturated carbon atoms of C–C, C–N, and OC–N, respectively (Table S1†). 50,51 The gradual upward trend of the N atom and the C–N bond content with increasing TGase was observed from the detailed quantitative compositional analysis and the relative peak area analysis of the Col and CPT groups, respectively (Table 1). These results provided support for the successful grafting of ε-PL into collagen fibrils in the CPTs owing to the introduction of extra ε-NH 2 from the amine groups in lysin segments of ε-PL.…”

Effects of Phenolics on the Physicochemical and Structural Properties of Collagen Hydrogel

“…In the thermogravimetric (TG) analysis, weight loss was observed in the initial stage (Δw1 = 6.5%, 99.8 °C) for all hydrogel samples. The weight loss during the specific temperature range was attributed to the release of two types of water states, namely, free and bound water, absorbed by the hydrogels [ 38 ]. Furthermore, the hydrogels treated with GA/EA lost less weight than the control group, implying that the presence of GA/EA reduced the water content of the collagen hydrogels due to the greater hydrophobicity of the phenolic compounds.…”

“…The second stage of weight loss was observed in all hydrogels at a temperature range of 228.3 °C–257.9 °C, with a weight loss percentage (Δw2) ranging from 2.6% to 9.7%. The weight loss at the second stage was typically associated with the release of structurally bound water and low molecular weight proteins, specifically collagen [ 38 ]. In conclusion, the thermal stability analysis reveals that the thermal degradation behavior of collagen hydrogels was influenced by the presence of phenolic compounds from GA/EA cross-linking.…”

Effects of ultrasound treatment on the morphological characteristics, structures and emulsifying properties of genipin cross-linked myofibrillar protein

“…Among these non-covalent interactions, hydrogen bond was the key force for the genipin binding to the MP through the number of residues and strength of the bond energy. In addition, numerous other studies have reported hydrogen bond as the main force for genipin-induced crosslinking, such as genipin-induced cross-linking of collagen-based fibrillar gels [34] and chitosan/silica composite films [35] . Moreover, Liu et al [36] also predicted that genipin was bound to the residues through hydrogen bond.…”