Sortase-tag expressed protein ligation: combining protein purification and site-specific bioconjugation into a single step.

ABSTRACT: Efficient labeling of protein-based targeting ligands with various cargos (drugs, imaging agents, nanoparticles, etc.) is essential to the fields of molecular imaging and targeted therapeutics. Many common bioconjugation techniques, however, are inefficient, nonstoichiometric, not site-specific, and/or incompatible with certain classes of protein scaffolds. Additionally, these techniques can result in a mixture of conjugated and unconjugated products, which are often difficult to separate. In this study, a bacterial sortase enzyme was utilized to condense targeting ligand purification and site-specific conjugation at the C-terminus into a single step. A model was produced to determine optimal reaction conditions for high conjugate purity and efficient utilization of cargo. As proof-of-prin

SUBMITTER: Warden-Rothman R 

PROVIDER: S-EPMC3843242 | biostudies-literature | 2013 Nov

REPOSITORIES: biostudies-literature