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

doi:10.1021/ja2004736

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

Chemistry

Research output: Contribution to journal › Article › peer-review

145 Scopus citations

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.

Original language	English (US)
Pages (from-to)	8392-8395
Number of pages	4
Journal	Journal of the American Chemical Society
Volume	133
Issue number	22
DOIs	https://doi.org/10.1021/ja2004736
State	Published - Jun 8 2011

ASJC Scopus subject areas

Chemistry(all)
Biochemistry
Catalysis
Colloid and Surface Chemistry

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10.1021/ja2004736

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AU - Chien, Miao Ping

AU - Thompson, Matthew P.

AU - Sinkovits, Robert S.

AU - Olson, Norman H.

AU - Baker, Timothy S.

AU - Gianneschi, Nathan C.

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AB - 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.

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Controlling and switching the morphology of micellar nanoparticles with enzymes

Abstract

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