SpyLigase peptide-peptide ligation polymerizes affibodies to enhance magnetic cancer cell capture.

ABSTRACT: Individual proteins can now often be modified with atomic precision, but there are still major obstacles to connecting proteins into larger assemblies. To direct protein assembly, ideally, peptide tags would be used, providing the minimal perturbation to protein function. However, binding to peptides is generally weak, so assemblies are unstable over time and disassemble with force or harsh conditions. We have recently developed an irreversible protein-peptide interaction (SpyTag/SpyCatcher), based on a protein domain from Streptococcus pyogenes, that locks itself together via spontaneous isopeptide bond formation. Here we develop irreversible peptide-peptide interaction, through redesign of this domain and genetic dissection into three parts: a protein domain termed SpyLigase, which now l

SUBMITTER: Fierer JO 

PROVIDER: S-EPMC3977242 | biostudies-literature | 2014 Apr

REPOSITORIES: biostudies-literature