Amphiphilic molecules form micelles when introduced into an aqueous environment. A micelle structure consists of hydrophobic tails at the core of the structure with hydrophilic peptide groups as the shell. Pharmaceuticals and biologics can be protected from absorption within the core of the micelle and the peptide itself can be used as a therapeutic making these peptide amphiphilic micelles ideal objects for drug delivery. When micelles are created they form either spherical or cylindrical shapes. The micelle shape is critical in drug delivery because smaller spherical micelles may pass through membranes, whereas larger cylindrical micelles may be ideal for tissue binding. This project aims to find the cause of the formation of micelle spheres versus micelle cylinders. This is done by using various sequences of peptide chains and hydrophobic tails to determine if either groups persuade the micelle to form a certain shape. The peptides are characterized using reverse phase high performance liquid chromatography (HPLC), mass spectrometry, and dynamic light scattering (DLS). Currently, data shows that C10(GSS)4 and C16P4(GSS)4 forms a cylindrical micelle. Future work consists of characterizing and comparing more micelles and then introducing these structures into a physiological setting. Measuring the stability of these different micelles is a critical factor in drug delivery.