Simulations of the erythrocyte cytoskeleton at large deformation. I. Microscopic models.
Three variations of a polymer chain model for the human erythrocyte cytoskeleton are used in large deformation simulations of microscopic membrane patches. Each model satisfies an experimental observation that the contour length of the spectrin tetramers making up the erythrocyte cytoskeleton is roughly square root of 7 times the end-to-end distance of the tetramer in vivo. Up to modest stress, each brushy cytoskeletal network behaves, consistently, like a low-temperature, planar network of Hookean springs, with a model-dependent effective spring constant, keff, in the range of 20-40 kBT/s(o)2, where T is the temperature and s(o) is the force-free spring length. However, several features observed at large deformation distinguish these models from spring networks: 1) Network dimensions do not expand without bound in approaching a critical isotropic tension (square root of 3 keff) that is a characteristic limit of Hookean spring nets. 2) In surface compression, steric interactions among the chain elements prevent a network collapse that is otherwise observed in compression of planar triangulated networks of springs. 3) Under uniaxial surface tension, isotropy of the network disappears only as the network is stretched by more than 50% of its equilibrium dimensions. Also found are definitively non-Hookean regimes in the stress dependence of the elastic moduli. Lastly, determinations of elastic moduli from both fluctuations and stress/strain relations prove to be consistent, implying that consistency should be expected among experimental determinations of these quantities.
Boey
S K
SK
Department of Physics, Simon Fraser University, Burnaby, British Columbia, Canada.
Boal
D H
DH
Discher
D E
DE
D016880:Anisotropy; D055592:Biophysical Phenomena; D001703:Biophysics; D003599:Cytoskeleton / Q000737:chemistry / Q000502:physiology*; D004548:Elasticity; D004907:Erythrocyte Deformability / Q000502:physiology*; D004912:Erythrocytes / Q000737:chemistry / Q000502:physiology*; D006801:Humans; D008954:Models, Biological; D011487:Protein Conformation; D013049:Spectrin / Q000737:chemistry / Q000502:physiology; D013314:Stress, Mechanical; D013500:Surface Tension
D013049:Spectrin