Insight into the effect of sulfonated chitosan on the structure, rheology and fibrillogenesis of collagen

As a heparin analogue, sulfonated chitosan (SCS) has been confirmed to have similar structure and properties to heparin which is shown to be a linker molecule having specific binding sites with collagen fibrils. In this study, the effects of a varying concentration of SCS on the self-assembly process of type 1 collagen were investigated. The study on intermolecular interaction between collagen and SCS was carried out via using ultraviolet-visible (UV-vis) spectrophotometry and circular dichroism (CD) spectroscopy. The addition of SCS did not disrupt the triple helix conformation of collagen. However, the decreased value of Rpn showed that the SCS, to some extent, influenced the percentage of triple helix conformation. The turbidity measurements revealed that the self-assembly rate was increased in the presence of a low concentration of SCS whereas decreased with further increasing the SCS concentration. The observation of microstructure via scanning electron microscopy (SEM) and atomic force microscopy (AFM) exhibited the characteristic D-periodicity, indicating that the presence of SCS did not disrupt the self-assembly nature of collagen. Moreover, the addition of SCS facilitated the lateral aggregation of fibrils, leading to the formation of larger fibrils. The rheological analysis showed that the gelation time of collagen was prolonged with increasing the concentration of SCS, in support of a longer lag-phase duration detected in turbidimetric measurements. We expect that valuable data would be provided in this study for further developing of ECM analogues, and propitious performances could be endowed to these biomimetic materials after SCS incorporation. (C) 2020 Published by Elsevier B.V.

Automated summary

Sulfonated chitosan (SCS) has similar structure and properties to heparin, acting as a linker molecule with specific binding sites on collagen fibrils. The addition of SCS did not disrupt the triple helix conformation of collagen but influenced its percentage to some extent. Self-assembly rate increased with low SCS concentration but decreased with higher concentrations.