Nanovesicles based on self-assembly of conformationally constrained aromatic residue containing amphiphilic dipeptides

Abstract

Peptide-based vesicular structures have been the focus of research in the past decade for their potential application as drug delivery agents. We here report the self-assembly of amphiphilic dipeptides containing conformation-constraining α , β -dehydrophenylalanine into nanovesicles. The vesicles can encapsulate small drug molecules such as riboflavin and vitamin B, bioactive peptides, and small protein molecules. The nanovesicles are resistant to treatment of a nonspecific protease, proteinase K, and are stable at low concentrations of monovalent and divalent cations. The vesicles are effectively taken up by actively growing cells in culture and show no observable cytopathic effects. These peptide-based nanostructures can be considered as models for further development as delivery agents for different biomolecules.