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Controlling and switching the morphology of micellar nanoparticles with enzymes.

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.

SUBMITTER: Ku TH

PROVIDER: S-EPMC3756928 | biostudies-literature | 2011 Jun

REPOSITORIES: biostudies-literature

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Controlling and switching the morphology of micellar nanoparticles with enzymes.

Ku Ti-Hsuan TH Chien Miao-Ping MP Thompson Matthew P MP Sinkovits Robert S RS Olson Norman H NH Baker Timothy S TS Gianneschi Nathan C NC

Journal of the American Chemical Society 20110404 22

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 reconstruct ...[more]

PMID: 21462979

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