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<p>In this study, fd bacteriophages were genetically reprogrammed to express a gold (Au) binding peptide (V5) on 2500 copies of the P8 major coat protein displayed on the virus body. The morphology of wild-type fd and engineered p8V5 viruses was studied by atomic force microscopy (AFM) topography measurements. The p8V5 phages retained their characteristic filamentous structure following genetic modification, with a dry state thickness of 2–3&#xa0;nm. Quartz crystal microbalance (QCM) analyses resulted in a net frequency change of 201.9 ± 16.1&#xa0;Hz for the p8V5 viruses, which was significantly higher than that observed for the wild-type phages (46.5 ± 8.7&#xa0;Hz) implying their enhanced Au surface binding. Gold nanoparticle (AuNP) binding of the viruses was studied using an aggregation interference test with 20&#xa0;nm PBS stabilized AuNPs. P8V5 treated AuNPs conserved their typical surface plasmon resonance band upon aggregation induction, suggesting enhanced AuNP stability through virus binding. UV–Vis absorption spectroscopy, scanning electron microscopy (SEM) and energy dispersive X-ray spectroscopy (EDX) analyses showed improved AuNP binding of the engineered p8V5 viruses, in line with the QCM measurements. A one-pot, citrate mediated Au metallization reaction was performed at room temperature using wild-type fd and recombinant p8V5 phages as biotemplates. The metallized samples were analyzed by SEM, EDX and AFM measurements. The P8 display of V5 peptides resulted in improved Au binding, forming densely packed metallized structures on engineered p8V5 virus filaments. Such engineered biomaterials with target specific affinities could be further applied as novel bioremediation agents in a circular economy.</p>

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Gold binding and mineralization by engineered bacteriophages

  • 期刊论文

  • 发表日期：

    2025年9月25日

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  • Nuriye Korkmaz,
  • Jihoon Kim

摘要

In this study, fd bacteriophages were genetically reprogrammed to express a gold (Au) binding peptide (V5) on 2500 copies of the P8 major coat protein displayed on the virus body. The morphology of wild-type fd and engineered p8V5 viruses was studied by atomic force microscopy (AFM) topography measurements. The p8V5 phages retained their characteristic filamentous structure following genetic modification, with a dry state thickness of 2–3 nm. Quartz crystal microbalance (QCM) analyses resulted in a net frequency change of 201.9 ± 16.1 Hz for the p8V5 viruses, which was significantly higher than that observed for the wild-type phages (46.5 ± 8.7 Hz) implying their enhanced Au surface binding. Gold nanoparticle (AuNP) binding of the viruses was studied using an aggregation interference test with 20 nm PBS stabilized AuNPs. P8V5 treated AuNPs conserved their typical surface plasmon resonance band upon aggregation induction, suggesting enhanced AuNP stability through virus binding. UV–Vis absorption spectroscopy, scanning electron microscopy (SEM) and energy dispersive X-ray spectroscopy (EDX) analyses showed improved AuNP binding of the engineered p8V5 viruses, in line with the QCM measurements. A one-pot, citrate mediated Au metallization reaction was performed at room temperature using wild-type fd and recombinant p8V5 phages as biotemplates. The metallized samples were analyzed by SEM, EDX and AFM measurements. The P8 display of V5 peptides resulted in improved Au binding, forming densely packed metallized structures on engineered p8V5 virus filaments. Such engineered biomaterials with target specific affinities could be further applied as novel bioremediation agents in a circular economy.