  Many proteins and peptides have an intrinsic capacity to sense and induce
membrane curvature, and play crucial roles for organizing and remodelling cell
membranes. However, the molecular driving forces behind these processes are not
well understood. Here, we describe a new approach to study curvature sensing,
by simulating the direction-dependent interactions of single molecules with a
buckled lipid bilayer. We analyse three amphipathic antimicrobial peptides, a
class of membrane-associated molecules that specifically target and destabilize
bacterial membranes, and find qualitatively different sensing characteristics
that would be difficult to resolve with other methods. These findings provide
new insights into the curvature sensing mechanisms of amphipathic peptides and
challenge existing theories of hydrophobic insertion. Our approach is generally
applicable to a wide range of curvature sensing molecules, and our results
provide strong motivation to develop new experimental methods to track position
and orientation of membrane proteins.
