Macrocyclic peptides self-assemble into robust vesicles with molecular recognition capabilities

Bioconjug Chem. 2014 Nov 19;25(11):1996-2003. doi: 10.1021/bc500367z. Epub 2014 Oct 7.

Abstract

In this study, we developed macrocyclic peptide building blocks that formed self-assembled peptide vesicles with molecular recognition capabilities. Macrocyclic peptides were significantly different from conventional amphiphiles, in that they could self-assemble into vesicles at very high hydrophilic-to-total mass ratios. The flexibility of the hydrophobic self-assembly segment was critical for vesicle formation. The unique features of this peptide vesicle system include a homogeneous size distribution, unusually small size, and robust structural and thermal stability. The peptide vesicles successfully entrapped a hydrophilic model drug, released the payload very slowly, and were internalized by cells in a highly efficient manner. Moreover, the peptide vesicles exhibited molecular recognition capabilities, in that they selectively bound to target RNA through surface-displayed peptides. This study demonstrates that self-assembled peptide vesicles can be used as strong intracellular delivery vehicles that recognize specific biomacromolecular targets.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Amino Acid Sequence
  • Drug Carriers / chemistry*
  • Drug Carriers / metabolism
  • HeLa Cells
  • Humans
  • Hydrophobic and Hydrophilic Interactions
  • Intracellular Space / metabolism
  • Macrocyclic Compounds / chemistry*
  • Models, Molecular
  • Molecular Sequence Data
  • Peptides / chemistry*
  • Peptides / metabolism
  • Protein Conformation
  • Protein Transport
  • Temperature

Substances

  • Drug Carriers
  • Macrocyclic Compounds
  • Peptides