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
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Research Support, N.I.H., Extramural
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Research Support, Non-U.S. Gov't
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Research Support, U.S. Gov't, Non-P.H.S.
MeSH terms
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Cyclic AMP-Dependent Protein Kinases / chemistry
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Cyclic AMP-Dependent Protein Kinases / pharmacology*
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Matrix Metalloproteinase 2 / chemistry
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Matrix Metalloproteinase 2 / pharmacology*
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Matrix Metalloproteinase 9 / chemistry
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Matrix Metalloproteinase 9 / pharmacology*
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Micelles*
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Microscopy, Electron, Transmission
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Models, Molecular
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Molecular Structure
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Nanoparticles / chemistry*
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Particle Size
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Protein Phosphatase 1 / chemistry
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Protein Phosphatase 1 / pharmacology*
Substances
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Micelles
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Cyclic AMP-Dependent Protein Kinases
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Protein Phosphatase 1
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Matrix Metalloproteinase 2
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Matrix Metalloproteinase 9