| 초록 |
There are a myriad of multiscale peptide and protein structures that have evolved to exhibit unique multiple functionalities in biological systems. Peptide display is based on the ability of biological systems to express the encoded polypeptides on a protein platform of bacteria, yeast, and bacteriophage. Here we express tandem polypeptide sequences comprising ZnS-binding and biotin-like peptides, LRRSSEAHNSIV and SHLLQHPQ, respectively, on the major capsid proteins of T7 bacteriophage. The specific binding of genetically modified T7 bacteriophage to the target materials is carefully examined. T7 bacteriophage has a very strong affinity to targets due to the multivalent interaction mediated by 415 copies of capsid proteins, as determined from surface plasmon resonance (SPR) analysis. We expect that the genetically engineered phage can play a saversatile biomolecular framework for the self-assembly of various organic and inorganic nanomaterials, and functional molecules. |
