Controlling and Switching the Morphology of Micellar Nanoparticles with Enzymes
Autor: | Matthew P. Thompson, Norman H. Olson, Ti-Hsuan Ku, Robert S. Sinkovits, Timothy S. Baker, Nathan C. Gianneschi, Miao-Ping Chien |
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Rok vydání: | 2011 |
Předmět: |
Models
Molecular Morphology (linguistics) Proteolysis Nanoparticle Biochemistry Micelle Article Catalysis Colloid and Surface Chemistry Microscopy Electron Transmission Protein Phosphatase 1 Amphiphile Copolymer medicine Organic chemistry Particle Size Protein kinase A Micelles Molecular Structure medicine.diagnostic_test Chemistry General Chemistry Cyclic AMP-Dependent Protein Kinases Matrix Metalloproteinase 9 Biophysics Matrix Metalloproteinase 2 Nanoparticles Particle size |
Zdroj: | Journal of the American Chemical Society. 133:8392-8395 |
ISSN: | 1520-5126 0002-7863 |
Popis: | 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. |
Databáze: | OpenAIRE |
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