Influence of multivalent nitrilotriacetic acid lipid-ligand affinity on the circulation half-life in mice of a liposome-attached His6-protein.

@article{Platt2010InfluenceOM,
  title={Influence of multivalent nitrilotriacetic acid lipid-ligand affinity on the circulation half-life in mice of a liposome-attached His6-protein.},
  author={Virginia M Platt and Zhaohua Huang and Limin Cao and Matthew R. Tiffany and Kareen Riviere and Francis C. Szoka},
  journal={Bioconjugate chemistry},
  year={2010},
  volume={21 5},
  pages={892-902}
}
Metal chelation-ligand interactions, such as occur between nitrilotriacetic acid (NTA)-nickel and multihistidines, enable the noncovalent attachment of histidine-modified proteins to liposomes and other particles. We compared three lipids: a mono-NTA lipid (ca. 10 microM affinity) and two tris-NTA lipid derivatives (ca. 3 nM and 0.2 nM affinity) in their ability to retain two different his(6)-containing proteins on NTA-liposomes in the presence of serum or plasma and after intravenous injection… CONTINUE READING
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