Journal
CHEMICAL COMMUNICATIONS
Volume 49, Issue 28, Pages 2873-2875Publisher
ROYAL SOC CHEMISTRY
DOI: 10.1039/c3cc40472b
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Funding
- NIH T32 [5T32EB005970]
- Dept. of Radiology
- AFOSR-PECASE [FA9550-11-1-0105]
- ARO [W911NF-11-1-0264]
- NIH [NIBIB 1R01EB011633]
- NIH Transformative Research Award [R01HL117326]
- NIH Director's New Innovator Award [1DP2OD008724]
- Henry & Camille Dreyfus Foundation
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Polymers of norbornenyl-modified peptide-based enzyme substrates have been prepared via ring-opening metathesis polymerization (ROMP). Peptides displayed on water-soluble homopolymers retain the ability to be enzymatically processed by a disease-associated enzyme. In contrast, when the peptides are densely arrayed on a nanoparticle derived from a self-assembled amphiphilic block-copolymer, they function with reduced activity as enzymatic substrates.
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