Lipid rafts serve as stable regions within the dynamic cell membrane that allow for localization of membrane proteins. The clustering of multiple membrane proteins increases the interaction with ligands outside the membrane, as shown in antigen receptor signaling. This project sought to emulate the lipid raft function inside self-assembling Ureido-pyrimidone (UPy) supramolecular stacks with the incorporation of UPy “guest” molecules. The guest molecules were synthesized with both methyl and dimethylheptyl substituents on the UPy moiety to explore how changes in molecular packing and hydrophobic interactions affect the incorporation of the guest molecules, and their stability, within the stack. The tail of the guest molecules contains functional groups for versatility, e.g. dye or peptide attachment. Microfluidic experiments were performed and the changing association constant of each target guest molecule was analyzed against control molecules not containing the UPy moiety. In the future, peptides will be coupled to the guest molecules for attachment of ligands to the supramolecular scaffold.