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Langmuir. 2009 Jan 20;25(2):657-60. doi: 10.1021/la803596q.

Controllable g5p-protein-directed aggregation of ssDNA-gold nanoparticles.

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  • 1Center for Functional Nanomaterials, and Biology Department, Brookhaven National Laboratory, Upton, New York 11973, USA.


We assembled single-stranded DNA (ssDNA) conjugated nanoparticles using the phage M13 gene 5 protein (g5p) as the molecular glue to bind two antiparallel noncomplementary ssDNA strands. The entire process was controlled tightly by the concentration of the g5p protein and the presence of double-stranded DNA. The g5p-ssDNA aggregate was disintegrated by hybridization with complementary ssDNA (C-ssDNA) that triggers the dissociation of the complex. Polyhistidine-tagged g5p was bound to nickel nitrilotriacetic acid (Ni2+-NTA) conjugated nanoparticles and subsequently used to coassemble the ssDNA-conjugated nanoparticles into multiparticle-type aggregates. Our approach offers great promise for designing biologically functional, controllable protein/nanoparticle composites.

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