Currently, the self-assembly of type-I collagen triple helices during the formation of microfibrils is not fully understood. Moreover, full understanding of this process could lead to advancements in synthetic collagen macrostructures. This model approximates the triple helices as rigid spherocylinder with a constant length to diameter ratio of 250. Therefore, the location and direction of the triple helices can be described by a midpoint and two angles each. Initially, rods are randomly generated and checked to ensure that excluded volume is taken into account. This project then uses simulating annealing techniques to find the global minimum Helmholtz free energy of solution. This is a function of the rod orientation that incorporates the liquid crystalline properties of type-I collagen. Specifically, the Helmholtz free energy is calculated using the orientation probability distribution assumed by Onsager. Furthermore, the basis for the liquid crystalline properties is the quadrapolar tensor order parameter calculated from the same probability distribution. The most stable conformation of rods indicates a shift from the random orientation but does not mimic the structure of a microfibril. Thus, without the incorporation of Coulombic forces, the liquid crystalline properties of type-I collagen do not resolve the structure of the microfibril.

Modeling the liquid crystalline properties of type-I collagen

247th National Meeting (2014)

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