Drug carriers play a critical role in pharmaceutical industries. Existing commercial drug carriers are typically chemically synthesized, causing them polydisperse in size, not biocompatible and making it difficult to functionalize for biological applications. These limitations have prompted an extensive effort to create drug carriers from other molecules. A powerful alternative to chemical synthesis is the expression of recombinant proteins through molecular biology. These proteins have the exact amino acid sequence as dictated and monodisperse in weight. They would allow the direct incorporation of specific motifs that mediate biological activities and permit morphology control through sequence design. In this study, we have chosen a naturally occurring plant protein oleosin, which are surfactant-like and can stabilize oil bodies, as a starting candidate, which has been demonstrated to self-assemble into a variety of nanostructures. The excellent hydrophilicity of recombinantly derived resilin offers unique opportunities in creating amphiphilic fusion proteins with other hydrophobic peptides to result in interesting morphology. First, we designed a family of fusion variants of oleosin and resilin-like-peptide (RLP). All protein variants were confirmed using mass spectrometry (MALDI-TOF) and the protein aggregate shape was analyzed using Dynamic light scattering (DLS). We used cryo-TEM to confirm self-assembled structure from fusion variants. We studied the morphology of different variants as a function of several factors. Our results indicate current oleosin-RLP variants would self-assemble into spherical vesicles and rod-like-micelles in a physiological buffer, with morphology dependent on hydrophobicity, geometry design, and solution chemistry. These findings advance our understanding of protein-based self-assembly systems. The successful demonstration of controlled assembly through fusion protein design offers promising directions for developing next-generation therapeutic delivery platforms.