title: Post-Translational Modification of Bionanoparticles as a Modular Platform for Biosensor Assembly.
abstract: Context driven biosensor assembly with modular targeting and detection moieties is gaining significant attentions. Although protein-based nanoparticles have emerged as an excellent platform for biosensor assembly, current strategies of decorating bionanoparticles with targeting and detection moieties often suffer from unfavorable spacing and orientation as well as bionanoparticle aggregation. Herein, we report a highly modular post-translational modification approach for biosensor assembly based on sortase A-mediated ligation. This approach enables the simultaneous modifications of the Bacillus stearothermophilus E2 nanoparticles with different functional moieties for antibody, enzyme, DNA aptamer, and dye decoration. The resulting easy-purification platform offers a high degree of targeting and detection modularity with signal amplification. This flexibility is demonstrated for the detection of both immobilized antigens and cancer cells.
authors.affiliation: Department of Chemical and Biomolecular Engineering, University of Delaware , Newark, Delaware 19716, United States.
authors.forename: Qing
authors.initials: Q
authors.lastname: Sun
authors.affiliation: Department of Chemical and Biomolecular Engineering, University of Delaware , Newark, Delaware 19716, United States.
authors.forename: Qi
authors.initials: Q
authors.lastname: Chen
authors.affiliation: Department of Chemical and Biomolecular Engineering, University of Delaware , Newark, Delaware 19716, United States.
authors.forename: Daniel
authors.initials: D
authors.lastname: Blackstock
authors.affiliation: Department of Chemical and Biomolecular Engineering, University of Delaware , Newark, Delaware 19716, United States.
authors.forename: Wilfred
authors.initials: W
authors.lastname: Chen
mesh_terms: D019881:Aminoacyltransferases / Q000737:chemistry; D000912:Antibodies, Neoplasm / Q000737:chemistry; D052157:Aptamers, Nucleotide / Q000737:chemistry; D001426:Bacterial Proteins / Q000737:chemistry / Q000378:metabolism*; D015374:Biosensing Techniques; D002469:Cell Separation; D003546:Cysteine Endopeptidases / Q000737:chemistry; D005456:Fluorescent Dyes / Q000737:chemistry; D015870:Gene Expression; D001411:Geobacillus stearothermophilus / Q000737:chemistry / Q000201:enzymology / Q000235:genetics; D006367:HeLa Cells; D006801:Humans; D008156:Luciferases / Q000737:chemistry; D018396:Mucin-1 / Q000235:genetics / Q000378:metabolism; D053758:Nanoparticles / Q000737:chemistry*; D009363:Neoplasm Proteins / Q000235:genetics / Q000378:metabolism; D011499:Protein Processing, Post-Translational; D011768:Pyruvate Dehydrogenase Complex / Q000737:chemistry / Q000378:metabolism*; D013205:Staphylococcal Protein A / Q000737:chemistry; D013211:Staphylococcus aureus / Q000737:chemistry; D013917:Thrombin / Q000032:analysis
chemical_list: D000912:Antibodies, Neoplasm; D052157:Aptamers, Nucleotide; D001426:Bacterial Proteins; D005456:Fluorescent Dyes; C060192:MUC1 protein, human; D018396:Mucin-1; D009363:Neoplasm Proteins; D011768:Pyruvate Dehydrogenase Complex; D013205:Staphylococcal Protein A; D008156:Luciferases; D019881:Aminoacyltransferases; C120542:sortase A; D013917:Thrombin; D003546:Cysteine Endopeptidases
keywords: bionanoparticles; biosensor; easy purification; modularity; post-translational modification; signal amplification