We are currently investigating the membrane effects of monomeric and oligomeric forms of Amyloid β (25-35) peptide. In order to regulate the growth of the oligomeric intermediates that have been implicated as the toxic form of the peptide, we have prepared the peptide using both D- and L- isomers of the amino acids. We wish to establish that both D and L forms interact with phospholipid membranes in exactly the same way and, therefore, wish to collect lamellar neutron diffraction data using well-established protocols, to supplement data from other biophysical techniques including circular dichroism, Langmiur balance and electrical conductance measurements.