An emerging field in biomaterials is the creation and engineering of protein surfactants made by recombinant biotechnology. Protein surfactants made by recombinant biotechnology allow for complete control of the molecular weight and chemical sequence of the surfactant. The proteins are monodisperse in molecular weight, and functionalization with bioactive amino acid sequences is straightforwardly achieved through genetic engineering. We modified the naturally occurring amphiphilic plant protein oleosin by truncating a large portion of its central hydrophobic block, creating a soluble triblock surfactant. Additional variants were constructed to eliminate secondary structure and create ionic surfactants. Variants of oleosin self-assembled into spherical micelles with a diameter of ?21 nm at concentrations above the critical micelle concentration (cmc). We found that the cmc could be manipulated through changes in the protein backbone and was correlated with changes in the protein secondary structure. Micelle size and shape are characterized with dynamic light scattering (DLS), small-angle X-ray scattering (SAXS), and cryogenic transmission electron microscopy (cryo-TEM). Micelles were functionalized with the integrin-binding domain, RGDS, leading to a 2.9-fold increase in uptake in Ovcar-5 cells after 12 h. Oleosin surfactants present a promising platform for micellar assembly because of the ability to precisely modify the protein backbone through molecular biology, allowing for the control over the cmc and the addition of functional domains into the materia.