Controlling and switching the morphology of micellar nanoparticles with enzymes

J Am Chem Soc. 2011 Jun 8;133(22):8392-5. doi: 10.1021/ja2004736. Epub 2011 Apr 4.

Abstract

Micelles were prepared from polymer-peptide block copolymer amphiphiles containing substrates for protein kinase A, protein phosphatase-1, and matrix metalloproteinases 2 and 9. We examine reversible switching of the morphology of these micelles through a phosphorylation-dephosphorylation cycle and study peptide-sequence directed changes in morphology in response to proteolysis. Furthermore, the exceptional uniformity of these polymer-peptide particles makes them amenable to cryo-TEM reconstruction techniques lending insight into their internal structure.

Publication types

  • Research Support, N.I.H., Extramural
  • Research Support, Non-U.S. Gov't
  • Research Support, U.S. Gov't, Non-P.H.S.

MeSH terms

  • Cyclic AMP-Dependent Protein Kinases / chemistry
  • Cyclic AMP-Dependent Protein Kinases / pharmacology*
  • Matrix Metalloproteinase 2 / chemistry
  • Matrix Metalloproteinase 2 / pharmacology*
  • Matrix Metalloproteinase 9 / chemistry
  • Matrix Metalloproteinase 9 / pharmacology*
  • Micelles*
  • Microscopy, Electron, Transmission
  • Models, Molecular
  • Molecular Structure
  • Nanoparticles / chemistry*
  • Particle Size
  • Protein Phosphatase 1 / chemistry
  • Protein Phosphatase 1 / pharmacology*

Substances

  • Micelles
  • Cyclic AMP-Dependent Protein Kinases
  • Protein Phosphatase 1
  • Matrix Metalloproteinase 2
  • Matrix Metalloproteinase 9