Controlling and Switching the Morphology of Micellar Nanoparticles with Enzymes

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...

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Bibliographic Details
Published in:Journal of the American Chemical Society 2011-06, Vol.133 (22), p.8392-8395
Main Authors: Ku, Ti-Hsuan, Chien, Miao-Ping, Thompson, Matthew P, Sinkovits, Robert S, Olson, Norman H, Baker, Timothy S, Gianneschi, Nathan C
Format: Article
Language:English
Subjects:
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
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Summary: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.
ISSN:0002-7863
1520-5126
DOI:10.1021/ja2004736