Abstract
Helical rosette nanotubes (HRN) are obtained through an entropically driven self-assembly process of low-molecular-weight synthetic modules under physiological conditions. Counter-intuitively, these materials undergo extensive self-assembly under the effect of temperature, resulting in networks of very long nanotubes. We have previously shown, using an in vitro model, that titanium (Ti) coated with HRN containing a lysine side chain (HRN-K1) displayed enhanced osteoblast (OB) adhesion when compared to uncoated Ti ( p<0.01). Because it has been widely known that proteins play a critical role in OB adhesion on nanophase materials, here we examine OB adhesion on heated (+T) and unheated (−T) HRN-K1-coated Ti under serum (+S, presence of proteins) and serum-free (–S, absence of proteins) conditions. The results demonstrated that (a) while proteins enhanced OB adhesion on +T HRN-K1-coated Ti, they had no effect on –T HRN-K1-coated Ti, suggesting an active role played by the rosette nanotubes in promoting OB adhesion, and (b) under –S conditions, +T HRN-K1 induced the same level of OB adhesion as uncoated Ti under +S conditions, suggesting that +T HRN-K1 acts as a protein substitute. Finally, transmission electron microscopy and atomic force microscopy studies of +T and –T HRN-K1-coated Ti revealed a significant change in surface coverage, density and hierarchical organization of the nanotubes upon heating, which was correlated with their ability to promote cell adhesion.
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