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Curvature-inducing proteins containing a Bin/Amphiphysin/Rvs domain oftenhave intrinsically disordered domains. Recent experiments have shown that thesedisordered chains enhance curvature sensing and generation. Here, we report onthe modification of protein-membrane interactions by disordered chains usingmeshless membrane simulations. The protein and bound membrane are modeledtogether as a chiral crescent protein rod with two excluded-volume chains. Asthe chain length increases, the repulsion between them reduces the cluster sizeof the proteins. It induces spindle-shaped vesicles and a transition betweenarc-shaped and circular protein assemblies in a disk-shaped vesicle. For flatmembranes, an intermediate chain length induces many tubules owing to therepulsion between the protein assemblies, whereas longer chains promoteperpendicular elongation of tubules. Moreover, protein rods with zero rodcurvature and sufficiently long chains stabilize the spherical buds. Forproteins with a negative rod curvature, an intermediate chain length induces arugged membrane with branched protein assemblies, whereas longer chains inducethe formation of tubules with periodic concave-ring structures.

Membrane shape deformation induced by curvature-inducing proteins consisting of chiral crescent binding and intrinsically disordered domains