We propose to use neutron reflection to characterise the position and shape of subtilin/lipid II pore complexes as well as to characterise the kinetics of subtilin-lipid II and subtilin-undecaprenyl pyrophosphate complex assembly. Floating lipid bilayers will be prepared using DMPC-d67 and lipid II. Subtilin will be introduced from solution and the interaction with lipid II characterised. DMPC and subtilin are both available in deuterated form making a range of contrasts possible. Using specular neutron reflection and contrasts or 0, 12.5, 42 and 100% D2O, the position of peptides in the membrane will be investigated in the absence and in the presence of specific molecular targets, lipid II and 11PP. Kinetics of antibiotic/target interaction will be sought to decouple pore-formation from cell wall inhibition during antimicrobial action.