![]() ![]() coli and to potentially avoid unwanted immunogenic problems. For many of these applications there has been a drive to move towards smaller antibody formats, both to allow efficient recombinant production in E. The ability to raise antibodies with high affinity and specificity to almost any biomolecular target has made antibodies essential components in many biomedical fields, both in diagnostics and in the active targeting of drugs and contrast agents for molecular imaging. ![]() These proteins are promising building blocks for the chemoselective functionalization via NCL of a broad range of nanoparticle scaffolds, including micelles, liposomes and dendrimers. ConclusionĪ novel procedure was developed to obtain soluble, well-folded single-domain antibodies with reactive C-terminal thioesters in good yields. These thioester-functionalized single-domain antibodies allowed synthesis of immunomicelles via native chemical ligation in a single step. On column purification and 2-mercapthoethanesulfonic acid (MESNA)-induced cleavage yielded single-domain antibodies with a reactive C-terminal MESNA thioester in good yields. coli allowed efficient production of correctly-folded single-domain antibody (sdAb)-intein fusions proteins. ![]() However, current methods to generate antibody fragments with C-terminal thioesters require cumbersome refolding procedures, effectively preventing application of NCL for antibody-mediated targeting and molecular imaging. Expression systems based on self-cleavable intein domains allow the generation of recombinant proteins with a C-terminal thioester, providing a unique handle for site-specific conjugation using native chemical ligation (NCL). Classical bioconjugation strategies for generating antibody-functionalized nanoparticles are non-specific and typically result in heterogeneous compounds that can be compromised in activity. ![]()
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