Hydrophobically
driven self-assembly is a well-understood principle
that has been shown to facilitate micelle formation. Although quite
useful, the library of structures accessible is limited to only a
few simplistic geometric configurations that are suboptimal for complex
applications. It is believed that other physical phenomena like hydrogen
bonding and electrostatic interactions can be exploited to complement
hydrophobic interactions allowing for the design of structurally complex,
aggregated micelles. To test this theory, ABC triblock peptide amphiphiles
comprising an application-specific peptide, a zwitterion-like peptide,
and a hydrophobic lipid were synthesized for which block sequence
modifications and order changes were used to investigate their impact
on micelle formation. The results provide significant evidence that
both hydrophobic and electrostatic driving forces influence the formation
of complex micellar structures. Specifically, hydrophobic self-assembly
facilitates individual micelle formation, whereas dipole electrostatic
interactions govern the association of micelle units into complex
architectures. Initial results indicate that there exists considerable
flexibility in the choice of application-specific peptide allowing
these structures to serve as a platform technology for a variety of
fields.