Protein-induced supramolecular disassembly of amphiphilic polypeptide nanoassemblies

J Am Chem Soc. 2015 Jun 17;137(23):7286-9. doi: 10.1021/jacs.5b04285. Epub 2015 Jun 2.

Abstract

Mimicking noncovalent interaction based processes in nature has been an important goal of supramolecular chemistry. Here, we report on amphiphilic polypeptides that self-assemble to form nanoscale supramolecular assemblies and are programmed to disassemble in response to a specific protein. Benzenesulfonamide and carbonic anhydrase have been chosen as the ligand and protein, respectively, to demonstrate this possibility. Since the amphiphilic nanoassembly sequesters hydrophobic guest molecules, the protein-specific disassembly event provides a protein-sensitive molecular release as well. We envision that the binding induced disassembly and guest release might open up new opportunities for the next generation of supramolecular assemblies for protein-specific delivery and diagnostics.

Publication types

  • Research Support, N.I.H., Extramural

MeSH terms

  • Benzenesulfonamides
  • Carbonic Anhydrases / chemistry*
  • Carbonic Anhydrases / metabolism
  • Molecular Conformation
  • Nanostructures / chemistry*
  • Particle Size
  • Peptides / chemistry
  • Peptides / metabolism*
  • Sulfonamides / chemistry
  • Sulfonamides / metabolism
  • Surface Properties
  • Surface-Active Agents / chemistry
  • Surface-Active Agents / metabolism*

Substances

  • Peptides
  • Sulfonamides
  • Surface-Active Agents
  • Carbonic Anhydrases