Abstract
Efficient and controlled release of peptides bound to polymeric reverse micelle assemblies can be achieved through the cooperative effects of disassembly and disruption of charge-charge interactions. Through the examination of various peptides and polymer architectures, we have identified the factors that affect the release efficiency of the electrostatically bound peptides. Peptide guests and polymers with a greater number of complementary charges result in less efficient release than peptides and polymers with lower numbers of charges. Interestingly, we find that the presence of adjacent charged groups on the monomeric unit of the polymer exhibits exceptionally low release efficiency, perhaps because of a chelate-like effect, even when the total polymer charge is lower. Overall, our findings inform the design principles for catch-and-release systems based on polymeric reverse micelles, which offer great versatility and tunability.