Nonlinear elasticity in biological gels

By C. Storm, Jennifer J. Pastore, F. MacKintosh, Tom C. Lubensky, P. Janmey. Nature, 2004

1,609 citations recorded by the source corpus.

The mechanical properties of soft biological tissues are essential to their physiological function and cannot easily be duplicated by synthetic materials. Unlike simple polymer gels, many biological materials—including blood vessels, mesentery tissue, lung parenchyma, cornea and blood clots—stiffen as they are strained, thereby preventing large deformations that could threaten tissue integrity. The molecular structures and design principles responsible for this nonlinear elasticity are unknown. Here we report a molecular theory that accounts for strain-stiffening in a range of molecularly distinct gels formed from cytoskeletal and extracellular proteins and that reveals universal stress–strain relations at low to intermediate strains. The input to this theory is the force–extension curve for individual semi-flexible filaments and the assumptions that biological networks composed of these filaments are homogeneous, isotropic, and that they strain uniformly. This theory shows that systems of filamentous proteins arranged in an open crosslinked mesh invariably stiffen at low strains without requiring a specific architecture or multiple elements with different intrinsic stiffness.

Subfields: Cell Biology, Genetics

View Paper: https://www.semanticscholar.org/paper/c65accc7773dd55ea8047fe1dc778f3381c615de

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Citations in the corpus

Local force and geometry sensing regulate cell functions (2006, background): “, in addition to the possible matrix stiffening that is caused by the physical activity of cell”
Fibrin Formation, Structure and Properties (2017, background): “This non-linearity is called strain hardening or strain stiffening and is a fundamental property of biological gel-like structures (Storm et al. 2005).”
Fibrin gels and their clinical and bioengineering applications (2009, methodology): “The persistence length of fibrin protofibrils is measured to be 500 nm (Storm et al. 2005), corresponding to Young’s modulus of 4 MPa taking the diameter of a protofibril to be 10 nm.”
Recent Advances in Bioink Design for 3D Bioprinting of Tissues and Organs (2017, background): “Cell suspension inks based on cell aggregates are a viable option to create scaffold-free biological constructs (Forgacs and Foty, 2004; Marga et al., 2007).”
Physical traits of cancer (2020, background): “Mechanical stresses can also alter the stiffness of the matrix through a phenomenon called strain-stiffening (101).”
A model for the contractility of the cytoskeleton including the effects of stress-fibre formation and dissociation (2007, background): “neglecting cell spreading and motility) have taken the perspective that the cytoskeleton is an interlinked structure of passive filaments (Satcher & Dewey 1996; Storm et al. 2005).”
Fibroblast adaptation and stiffness matching to soft elastic substrates. (2007, background): “Because of the nonlinear elasticity of many biopolymer networks, imposition of internal tension can lead to changes in stiffness even in the absence of changes in assembly (25,26).”
A review of nonlinear oscillatory shear tests: Analysis and application of large amplitude oscillatory shear (LAOS) (2011, background): “F-actin, fibrin, collagen, also show strain hardening behavior [84].”
Cell mechanics and the cytoskeleton (2010, neutral): “When shear stresses are applied to actin-filament networks, as well as to networks of intermediate filaments or extracellular-matrix filaments such as collagen and fibrin, the networks stiffen and resist additional deformation, as a result of filament entanglement (in which the displacement of one f”
Cell mechanics: integrating cell responses to mechanical stimuli. (2007, background): “Whereas some biopolymers such as elastin have elastic properties very similar to rubber-like materials (29, 30), gels formed by stiffer filaments, such as fibrin, collagen, actin, and intermediate filaments, have distinct rheological properties (28, 31).”
Actin-binding proteins sensitively mediate F-actin bundle stiffness (2006, background): “A mechanistic understanding of the effects of ABPs on F-actin bundle mechanics might thus be needed to obtain a complete understanding of their physiological role in cell”