Our group studies the interaction between antibiotic peptides and phospholipids. These peptides are known to form channels in the lipid membrane. With X-ray diffraction, oriented circular dichroism and in-plane neutron scattering measurements, and evidences from experiments done by others, we have established channel models for alamethicin and magainin, and measured the channel sizes. In this thesis, neutron off-plane scattering of aligned peptide-lipid samples is discussed. Compared to in-plane scattering, this new technique provides a much richer structural information of the sample. We therefore are able to easily distinguish different structures based on the scattering pattern, and, ideally, reconstruct the channel scattering length density in real space. Inter-membrane correlation was observed in the magainin samples.