Negatively
charged Ludox silica nanoparticles (SiNPs) form a complex
with atelocollagen (AC) in acidic buffers (pH = 4 or 3). AC is a low-immunogenic
derivative of collagen obtained by the removal of N- and C-terminal
telopeptide components. Mixed solutions of negatively charged SiNPs
and AC were turbid, while positively charged SiNPs (Ludox CL) did
not form a complex with AC in pH 4 buffer, indicating that electrostatic
attraction is the dominant force to form the complex. Small-angle
X-ray scattering (SAXS) and circular dichroism (CD) measurements were
made for AC and Ludox LS (or CL) solutions in acetate buffer (pH 4.0)
and citrate buffer (pH 3.0). The CD data showed that the stability
of the triple helical structure of AC in the buffers is not affected
by the complexation. The resulting complex consisting of triple helical
AC and SiNPs did not influence the SAXS profile except for the lowest q region investigated. On the contrary, different scattering
profiles were observed for the single chain AC and SiNP mixture indicating
densely packed SiNPs in the complex. This scattering behavior was
fairly explained in terms of the sticky hard sphere model (SHSM).
This AC conformation-dependent complexation may be because of the
hydrogen bonding interaction between the single chain AC and SiNPs.
The temperature-induced change of the complex formation can be applied
for thermoresponsive hybrid materials.