title: Bilayer elasticity at the nanoscale: the need for new terms.
abstract: Continuum elastic models that account for membrane thickness variations are especially useful in the description of nanoscale deformations due to the presence of membrane proteins with hydrophobic mismatch. We show that terms involving the gradient and the Laplacian of the area per lipid are significant and must be retained in the effective Hamiltonian of the membrane. We reanalyze recent numerical data, as well as experimental data on gramicidin channels, in light of our model. This analysis yields consistent results for the term stemming from the gradient of the area per molecule. The order of magnitude we find for the associated amplitude, namely 13-60 mN/m, is in good agreement with the 25 mN/m contribution of the interfacial tension between water and the hydrophobic part of the membrane. The presence of this term explains a systematic variation in previously published numerical data.
authors.affiliation: Laboratoire Matière et Systèmes Complexes, Université Paris Diderot, Paris 7, Sorbonne Paris Cité, CNRS UMR 7057, Paris, France.
authors.forename: Anne-Florence
authors.initials: AF
authors.lastname: Bitbol
authors.forename: Doru
authors.initials: D
authors.lastname: Constantin
authors.forename: Jean-Baptiste
authors.initials: JB
authors.lastname: Fournier
mesh_terms: D000465:Algorithms; D002462:Cell Membrane / Q000737:chemistry / Q000648:ultrastructure; D055119:Elastic Modulus; D006096:Gramicidin / Q000737:chemistry; D057927:Hydrophobic and Hydrophilic Interactions; D007473:Ion Channels / Q000737:chemistry; D008051:Lipid Bilayers; D008954:Models, Biological; D049329:Nanostructures; D055550:Protein Stability
chemical_list: D007473:Ion Channels; D008051:Lipid Bilayers; D006096:Gramicidin