Abstract
Some proteins and peptides have an intrinsic capacity to remodel lipid bilayers and sense membrane curvature via a curvature-dependent membrane binding energy. This is crucial for many biological processes. For example, antimicrobial peptides are believed to disrupt bacterial membranes by producing pores, which are highly curved structures. In this work, we explore a new computational method to investigate curvature sensing by simulating the interaction of single peptides with a buckled lipid bilayer, using the coarse-grained Martini model. We analyze three canonical antimicrobial peptides, magainin, melittin, and LL-37, and find qualitatively different sensing characteristics. In particular, melittin and LL-37 show anisotropic curvature sensitivity, but with different preferred orientations relative to the direction of greatest curvature. These findings provides new insights into the microscopic mechanisms of curvature sensing and its role in membrane remodeling, and should motivate experimental development to simultaneously measure position and orientation of membrane-bound proteins.
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