Surface selective binding of nanoclay particles to polyampholyte protein chains

Binding of nanoclay (Laponite) to gelatin-A and gelatin-B (both polyampholytes) molecules was investigated at room temperature (25 degrees C) both experimentally and theoretically. The stoichiometric binding ratio between gelatin and Laponite was found to be strongly dependent on the solution ionic strength. Large soluble complexes were formed at higher ionic strengths of the solution, a result supported by data obtained from light scattering, viscosity, and zeta potential measurements. The binding problem was theoretically modeled by choosing a suitable two-body screened Coulomb potential, U(R+)=(q(-)/2 epsilon)[(Q(-)/R-)e(-)(-kR)-(Q(+)/R+)e(+)(-kR)], where the protein dipole has charges Q(+) and Q(_) that are located at distances R+ and R-_ from the point Laponite charge q(-) and the dispersion liquid has dielectric constant (epsilon). U(R+) accounted for electrostatic interactions between a dipole (protein molecule) and an effective charge (Laponite particle) located at an angular position theta. Gelatin-A and Laponite association was facilitated by a strong attractive interaction potential that led to preferential binding of the biopolymer chains to negatively charged face of Laponite particles. In the case of gelatin-B selective surf ace patch binding dominated the process where the positively charged rim and negatively charged face of the particles were selectively bound to the oppositely charged segments of the biopolymer. The equilibrium separation (R-e) between the protein and nanoclay particle revealed monovalent salt concentration dependence given by R-e similar to[NaCl](alpha) where alpha=0.6 +/- 0.2 for gelatin-A and alpha=0.4 +/- 0.2 for gelatin-B systems. The equilibrium separations were approximate to 30% less compared to the gelatin-A system implying preferential short-range ordering of the gelatin-B-nanoclay pair in the solvent.