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Article Dans Une Revue Soft Matter Année : 2021

Binding of thermalized and active membrane curvature-inducing proteins

Résumé

Using analytical and numerical approaches, we find that equilibrium binding of membrane curving proteins on a membrane generates a phase-separated and corrugated phase. Active binding shifts its stability and makes the protein aggregates porous. The phase behavior of a membrane induced by the binding of curvature-inducing proteins is studied by a combination of analytical and numerical approaches. In thermal equilibrium under the detailed balance between binding and unbinding, the membrane exhibits three phases: an unbound uniform flat phase (U), a bound uniform flat phase (B), and a separated/corrugated phase (SC). In the SC phase, the bound proteins form hexagonally-ordered bowl-shaped domains. The transitions between the U and SC phases and between the B and SC phases are second order and first order, respectively. At a small spontaneous curvature of the protein or high surface tension, the transition between B and SC phases becomes continuous. Moreover, a first-order transition between the U and B phases is found at zero spontaneous curvature driven by the Casimir-like interactions between rigid proteins. Furthermore, nonequilibrium dynamics is investigated by the addition of active binding and unbinding at a constant rate. The active binding and unbinding processes alter the stability of the SC phase.

Dates et versions

hal-03228275 , version 1 (18-05-2021)

Identifiants

Citer

Quentin Goutaland, Frédéric van Wijland, Jean-Baptiste Fournier, Hiroshi Noguchi. Binding of thermalized and active membrane curvature-inducing proteins. Soft Matter, 2021, 17 (22), pp.5560-5573. ⟨10.1039/D1SM00027F⟩. ⟨hal-03228275⟩
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