Redox-active nanoscale materials such as porphyrin binding proteins are of immense interest because of their potential use in light-energy harvesting processes, hydrogen production/conversion or as bioelectronic devices. To realize this potential, we are designing simple, robust peptides (maquettes) with ligation sites that can position redox cofactors with angstrom level accuracy. We pattern the exterior of the maquettes to have overall amphiphilic character which leads to self-assembly in membranes and detergent micelles, at air-liquid interfaces, or on electrodic surfaces. We pattern the interior of the maquettes with hydrophobic amino acids for assembly into four-helix bundles. We place multiple histidines into the maquettes' interior to create chain of cofactors for electron transfer within the protein. We have prepared AP maquettes with up to 6 binding sites for protoporphyrins and tested how the position of the binding site with respect to the membrane affects the assembly, affinity, and redox properties. We investigated the functionality of the maquettes by measurements of electron transfer across membrane using stop flow kinetic approach and across lipid monolayer deposited on conductive substrate (HOPG) using Scanning Probe Microscopy (SPM).