Puroindolines are basic, cysteine rich proteins of ~13KDa, which have attracted significant interest due to their role in determining the endosperm texture of Wheat and seed defense. The antibacterial activity of both Pin-a and -b has been shown to be related to their ability form ion channels across both fungi and bacterial membranes. Pin-a is highly organized in solution, which is unusual for lipid binding/membrane proteins and suggests at the pathogenic membrane interface the protein is able to reorganize itself to enable penetration across the bilayer. Here, we wish to use neutron reflection to examine the interaction of Pin-a with both lipid monolayers and floating bilayers. We will use examine the interaction of Pin-a with model bilayers and monolayers of DPPG, Gaining insights into the activity of this biotechnologically important protein family.