Electrostatic effects in collagen fibril formation

Using light scattering and Atomic Force Microscopy techniques, we have studied the kinetics and equilibrium scattering intensity of collagen association, which is pertinent to the vitreous of the human eye. Specifically, we have characterized fibrillization dependence on pH, temperature, and ionic strength. At higher and lower pH, collagen triple helices remain stable in solution without fibrillization. At physiological pH, fibrillization occurs and the fibril growth is slowed upon either an increase in ionic strength or a decrease in temperature. The total light scattering with respect to ionic strength is non-monotonic in these conditions as a result of a competing dependence of fibril concentration and size on ionic strength. Fibril concentration is the highest at lower ionic strengths and rapidly decays for higher ionic strengths. On the other hand, fibril size is larger in solutions with higher ionic strength. We present a theoretical model, based on dipolar interactions in solutions, to describe the...