(115b) Protein Vesicles: Tuning Self-Assembly By Sequence Modifications | AIChE

(115b) Protein Vesicles: Tuning Self-Assembly By Sequence Modifications

Protein vesicles incorporating functional, globular proteins have potential in a number of bio-applications such as drug delivery, biocatalysis, and sensing. We have previously self-assembled protein vesicles from mCherry-zipper-ELP protein complexes where ELP is a thermo-responsive elastin-like polypeptide, zipper is a coiled-coil, and mCherry is a model folded protein. As we utilize these vesicles in different applications with different folded proteins, there is a need to control their size, stability, and stimuli responsiveness. We have modified the ELP amino acid sequence to introduce residues of varying hydrophobicity and charge and to create longer and shorter ELP sequences. ELP sequence significantly impacts the thermal induced hydrophobic transition of ELP and subsequent self-assembly of vesicles. I will discuss the roles of hydrophobicity and geometry in self-assembly and on the properties of vesicles formed. The wide range of vesicle properties enable application of protein vesicles as versatile functional and responsive protein materials.