3 years ago

Domains in mixtures of amphiphilic macromolecules with different stiffness of backbone

Domains in mixtures of amphiphilic macromolecules with different stiffness of backbone
The domain structuring in concentrated mixtures of amphiphilic macromolecules with a different stiffness of backbone has been discovered and studied by means of molecular dynamics simulation. The macromolecules were composed of identical amphiphilic H-graft-P monomer units. In flexible macromolecules, the H-graft-P units are connected freely, whereas the stiff macromolecules have limitations imposed on torsion and bending angles and carry local helical structure. In solvent which is poor for the backbone, stiff macromolecules form filament clusters from few intertwined helical chains. The filaments can be aligned along each other sharing a common director or form a few liquid-crystalline domains oriented randomly with respect to each other. It was shown that increase of fraction of helical macromolecules leads to decrease of order parameter and its high variation over different samples due to the increase of length and polydispersity of persistent filaments.

Publisher URL: www.sciencedirect.com/science

DOI: S0032386117307747

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