Inelastic mechanics: A unifying principle in biomechanics

Biochim Biophys Acta. 2015 Nov;1853(11 Pt B):3025-37. doi: 10.1016/j.bbamcr.2015.06.017. Epub 2015 Jul 4.

Abstract

Many soft materials are classified as viscoelastic. They behave mechanically neither quite fluid-like nor quite solid-like - rather a bit of both. Biomaterials are often said to fall into this class. Here, we argue that this misses a crucial aspect, and that biomechanics is essentially damage mechanics, at heart. When deforming an animal cell or tissue, one can hardly avoid inducing the unfolding of protein domains, the unbinding of cytoskeletal crosslinkers, the breaking of weak sacrificial bonds, and the disruption of transient adhesions. We classify these activated structural changes as inelastic. They are often to a large degree reversible and are therefore not plastic in the proper sense, but they dissipate substantial amounts of elastic energy by structural damping. We review recent experiments involving biological materials on all scales, from single biopolymers over cells to model tissues, to illustrate the unifying power of this paradigm. A deliberately minimalistic yet phenomenologically very rich mathematical modeling framework for inelastic biomechanics is proposed. It transcends the conventional viscoelastic paradigm and suggests itself as a promising candidate for a unified description and interpretation of a wide range of experimental data. This article is part of a Special Issue entitled: Mechanobiology.

Keywords: Cell aggregates; Cytoskeleton; Glassy wormlike chain; In-vitro biopolymer networks; Inelastic biomechanics; Microrheology; Rheological models; Soft glassy rheology; Structural plasticity; Transient crosslinkers.

Publication types

  • Research Support, Non-U.S. Gov't
  • Review

MeSH terms

  • Animals
  • Cell Membrane / chemistry*
  • Cell Membrane / metabolism
  • Cytoskeleton / chemistry*
  • Cytoskeleton / metabolism
  • Humans
  • Membrane Proteins / chemistry*
  • Membrane Proteins / metabolism
  • Models, Chemical*
  • Protein Structure, Tertiary

Substances

  • Membrane Proteins