Journal
ACS CHEMICAL BIOLOGY
Volume 11, Issue 8, Pages 2320-2327Publisher
AMER CHEMICAL SOC
DOI: 10.1021/acschembio.6b00444
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Funding
- National Science Foundation [CHE 1011796]
- National Institute of Health [GM101421, 1S10OD010603]
- Skaggs Institute for Chemical Biology
- Georgia Institute of Technology (Petit Institute Collaborative Seed Grant Program)
- NSF Graduate Research Fellowship Program
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Oxanorbornadiene dicarboxylate (OND) reagents were explored for the purpose of binding and releasing chemical cargos from endogenous circulating serum albumins. ONDs bearing gadolinium chelates as model cargos exhibited variable conjugation efficiencies with albumin in rat subjects that are consistent with the observed reactivity of each linker and their observed stability toward serum hydrolases in vitro. The terminal elimination rate from circulation was dependent on the identity of the OND used, and increased circulation time of gadolinium cargo was achieved for linkers bearing electrophilic fragments designed to react with cysteine-34 of circulating serum albumin. This binding of and release from endogenous albumin highlights the potential of OND linkers in the context of optimizing the pharmacokinetic parameters of drugs or diagnostic agents.
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