Nanovesicles based on self-assembly of conformationally constrained aromatic residue containing amphiphilic dipeptides.
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 alpha,beta-dehydrophenylalanine into nanovesicles. The vesicles can encapsulate small drug molecules such as riboflavin and vitamin B(12), 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.
Mishra
Aseem
A
International Centre for Genetic Engineering and Biotechnology, New Delhi, and National Institute of Virology, Pune, India.
Panda
Jiban Jyoti
JJ
Basu
Atanu
A
Chauhan
Virander Singh
VS
D002214:Capsules / Q000737:chemistry / Q000633:toxicity; D002470:Cell Survival / Q000187:drug effects; D002942:Circular Dichroism; D004151:Dipeptides / Q000138:chemical synthesis / Q000737:chemistry*; D006367:HeLa Cells; D006801:Humans; D057927:Hydrophobic and Hydrophilic Interactions; D046529:Microscopy, Electron, Transmission; D053758:Nanoparticles / Q000737:chemistry* / Q000633:toxicity / Q000648:ultrastructure; D017550:Spectroscopy, Fourier Transform Infrared; D014867:Water / Q000737:chemistry*
D002214:Capsules; D004151:Dipeptides; D014867:Water