A novel strain energy relationship for red blood cell membrane skeleton based on spectrin stiffness and its application to micropipette deformation.

Abstract

Red blood cell (RBC) membrane skeleton is a closed two-dimensional elastic network of spectrin tetramers with nodes formed by short actin filaments. Its three-dimensional shape conforms to the shape of the bilayer, to which it is connected through vertical linkages to integral membrane proteins. Numerous methods have been devised over the years to predict the response of the RBC membrane to applied forces and determine the corresponding increase in the skeleton elastic energy arising either directly from continuum descriptions of its deformation, or seeking to relate the macroscopic behavior of the membrane to its molecular constituents. In the current work, we present a novel continuum formulation rooted in the molecular structure of the membrane and apply it to analyze model deformations similar to those that occur during aspiration of RBCs into micropipettes. The microscopic elastic properties of the skeleton are derived by treating spectrin tetramers as simple linear springs. For a given local deformation of the skeleton, we determine the average bond energy and define the corresponding strain energy function and stress-strain relationships. The lateral redistribution of the skeleton is determined variationally to correspond to the minimum of its total energy. The predicted dependence of the length of the aspirated tongue on the aspiration pressure is shown to describe the experimentally observed system behavior in a quantitative manner by taking into account in addition to the skeleton energy an energy of attraction between RBC membrane and the micropipette surface.