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

Soo Kwan Lee; Mathew M. Maye; Yian Biao Zhang; Oleg Gang; Daniel Van Der Lelie

doi:10.1021/la803596q

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

Soo Kwan Lee, Mathew M. Maye, Yian Biao Zhang, Oleg Gang, Daniel Van Der Lelie

Research output: Contribution to journal › Article › peer-review

23 Scopus citations

Abstract

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 (Ni ²⁺-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.

Original language	English (US)
Pages (from-to)	657-660
Number of pages	4
Journal	Langmuir
Volume	25
Issue number	2
DOIs	https://doi.org/10.1021/la803596q
State	Published - Jan 20 2009
Externally published	Yes

ASJC Scopus subject areas

General Materials Science
Condensed Matter Physics
Surfaces and Interfaces
Spectroscopy
Electrochemistry

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10.1021/la803596q

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abstract = "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 (Ni 2+-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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AU - Maye, Mathew M.

AU - Zhang, Yian Biao

AU - Gang, Oleg

AU - Van Der Lelie, Daniel

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AB - 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 (Ni 2+-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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Controllable g5p-protein-directed aggregation of ssDNA-gold nanoparticles

Abstract

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