Investigation on the behavior of collagen self-assembly in vitro via adding sodium silicate.

Silicon, a trace element found in human body, plays a critical role in the process of collagen self-assembly. In this study, the intermolecular interaction and fibrillogenesis process were investigated to understand the effects of various concentrations of sodium silicate (SS) on collagen self-assembly in vitro. Fourier transform infrared spectroscopy analysis indicated that the triple helical structure of collagen was not significantly affected by SS. Hydrophobic interactions and particle sizes of collagen aggregates, which were measured using pyrene fluorescence and dynamic light scanning, enhanced via adding 2 mM SS whereas decreased with further increasing concentrations (4-8 mM). Kinetic analysis revealed that an increase in hydrophobic interactions boosted collagen self-assembly in the presence of 2 mM SS. The inhibition of self-assembly with the addition of 4-8 mM SS, as illustrated by a reduction in the fibrillogenesis rate and turbidity, was potentially attributed to weak hydrophobic interactions and strong electrostatic repulsion. The observation of microscopy demonstrated that the fibrils exhibited the characteristic D-periodicity at 2 mM SS. The inhibitory effect of 4 mM SS was slight and the fibrils still formed, while the microstructure was consisted of clustered collagen aggregates as SS ≥ 6 mM owing to serious inhibition on collagen self-assembly.