4.8 Article

Nanoparticles Self-Assembly Driven by High Affinity Repeat Protein Pairing

Journal

ACS NANO
Volume 10, Issue 3, Pages 3176-3185

Publisher

AMER CHEMICAL SOC
DOI: 10.1021/acsnano.5b04531

Keywords

alpha-repeat proteins; gold nanoparticles; reversible self-assembly; protein pair; dissociation constant

Funding

  1. European Research Council (ERC), CNRS High Risk Program NanoBriques [FP7-ERC-2007-StG-203872]
  2. Agence Nationale de la Recherche (ANR) [ANR-14-CE08-0004-ARTEMIS]

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Proteins are the most specific yet versatile biological self-assembling agents with a rich chemistry. Nevertheless, the design of new proteins with recognition capacities is still in its infancy and has seldom been exploited for the self-assembly of functional inorganic nanoparticles. Here, we report on the protein directed assembly of gold nanoparticles using purpose-designed artificial repeat proteins having a rigid but modular 3D architecture. alpha Rep protein pairs are selected for their high mutual affinity from a library of 10(9) variants. Their conjugation onto gold nanoparticles drives the massive colloidal assembly of free-standing, one-particle thick films. When the average number of proteins per nanoparticle is lowered, the extent of self-assembly is limited to oligomeric particle clusters. Finally, we demonstrate that the aggregates are reversibly disassembled by an excess of one free protein. Our approach could be optimized for applications in biosensing, cell targeting, or functional nanomaterials engineering.

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