Controlling and switching the morphology of micellar nanoparticles with enzymes

Ti Hsuan Ku, Miao Ping Chien, Matthew P. Thompson, Robert S. Sinkovits, Norman H. Olson, Timothy S. Baker, Nathan C. Gianneschi

Research output: Contribution to journalArticlepeer-review

145 Scopus citations


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.

Original languageEnglish (US)
Pages (from-to)8392-8395
Number of pages4
JournalJournal of the American Chemical Society
Issue number22
StatePublished - Jun 8 2011

ASJC Scopus subject areas

  • Chemistry(all)
  • Biochemistry
  • Catalysis
  • Colloid and Surface Chemistry


Dive into the research topics of 'Controlling and switching the morphology of micellar nanoparticles with enzymes'. Together they form a unique fingerprint.

Cite this