Journal
JOURNAL OF THE AMERICAN CHEMICAL SOCIETY
Volume 133, Issue 22, Pages 8392-8395Publisher
AMER CHEMICAL SOC
DOI: 10.1021/ja2004736
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Funding
- University of California, a Camille & Henry Dreyfis Foundation
- DOD-AFOSR
- NIH [1S10 RR020016, R37 GM-033050, R01 AI-079095]
- UCSD
- Division Of Chemistry
- Direct For Mathematical & Physical Scien [0741968] Funding Source: National Science Foundation
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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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