Journal
BIOMACROMOLECULES
Volume 13, Issue 7, Pages 2099-2109Publisher
AMER CHEMICAL SOC
DOI: 10.1021/bm3004836
Keywords
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Funding
- Department of Energy [DE-SC0005166]
- Baystate Health Systems (Springfield, MA)
- National Science Foundation [CBET-0932781]
- National Science Foundation through a Graduate Research Fellowship
- [06-4]
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Novel pentafluorophenyl (PFP)-ester-functionalized phosphorylcholine (PC) polymers of different architectures were prepared and conjugated to lysozyme as a model protein. Linear and two-arm poly(2-methacryloyloxyethyl phosphorylcholine) (polyMPC) structures containing PFP functionality at the chain-end were prepared by atom transfer radical polymerization (ATRP) from novel initiators. Additional conjugates were prepared from phosphorylcholine-substituted cyclooctene (PC-COE) polymers containing PFP-ester bearing comonomers. The polymer-protein conjugates were characterized by HPLC, FPLC, and DLS and were seen to retain most (similar to 80% or greater) of their native enzymatic activity. Pharmacokinetic profiles of the polymer-protein conjugates were studied in mice and found to increase the circulation half-life compared with lysozyme alone.
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