Dependence of protein-induced lipid bilayer deformations on protein shape

TL;DR

This paper introduces a boundary value method (BVM) for non-perturbative analytic solutions of lipid bilayer deformations caused by membrane proteins with various shapes, advancing understanding of protein-membrane interactions.

Contribution

The paper develops a novel boundary value method enabling exact solutions for lipid bilayer deformations induced by non-circular membrane proteins, extending beyond previous idealized models.

Findings

BVM reproduces known solutions for circular proteins.

Excellent agreement with finite element numerical solutions for non-circular shapes.

Analytic approximation effectively predicts deformation energy for modest shape deviations.

Abstract

Membrane proteins typically deform the surrounding lipid bilayer membrane, which can play an important role in the function, regulation, and organization of membrane proteins. Membrane elasticity theory provides a beautiful description of protein-induced lipid bilayer deformations, in which all physical parameters can be directly determined from experiments. Analytic treatments of the membrane elasticity theory of protein-induced lipid bilayer deformations have largely focused on idealized protein shapes with circular cross section, and on perturbative solutions for proteins with non-circular cross section. We develop here a boundary value method (BVM) that permits the construction of non-perturbative analytic solutions of protein-induced lipid bilayer deformations for non-circular protein cross sections, for constant as well as variable boundary conditions along the bilayer-protein interface. We apply this BVM to protein-induced lipid bilayer thickness deformations. Our BVM reproduces available analytic solutions for proteins with circular cross section and yields, for proteins with non-circular cross section, excellent agreement with numerical, finite element solutions. On this basis, we formulate a simple analytic approximation of the bilayer thickness deformation energy associated with general protein shapes and show that, for modest deviations from rotational symmetry, this analytic approximation is in good agreement with BVM solutions. Using the BVM, we survey the dependence of protein-induced lipid bilayer thickness deformations on protein shape, and thus explore how the coupling of protein shape and bilayer thickness deformations affects protein oligomerization and transitions in protein conformational state.