We have shown that asymmetric amphiphiles unexpectedly self-assemble into a cylindrical morphology, despite their very high hydrophilic weight fraction. Additionally, we have used their recombinant design to show that their self-assembly can be precisely tuned by varying the length of the ELP block, the hydrophobicity of the amino acid X, and the number of glycine spacers z, enabling asymmetric amphiphile self-assembly to be specifically tuned for a desired drug delivery application. The morphological diversity within this subset of amphiphiles suggests that there may be vast and as-of-yet unexplored regions of sequence space with morphological diversity. Future studies will explore these regions, as well as address more fundamental questions regarding the mechanism of self-assembly for asymmetric amphiphiles.
展开▼
