Nanoparticles Self-Assembly Driven by High Affinity Repeat Protein Pairing

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 repor...

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Veröffentlicht in:ACS nano 2016-03, Vol.10 (3), p.3176-3185
Hauptverfasser: Gurunatha, Kargal L, Fournier, Agathe C, Urvoas, Agathe, Valerio-Lepiniec, Marie, Marchi, Valérie, Minard, Philippe, Dujardin, Erik
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container_end_page 3185
container_issue 3
container_start_page 3176
container_title ACS nano
container_volume 10
creator Gurunatha, Kargal L
Fournier, Agathe C
Urvoas, Agathe
Valerio-Lepiniec, Marie
Marchi, Valérie
Minard, Philippe
Dujardin, Erik
description 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. αRep protein pairs are selected for their high mutual affinity from a library of 109 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.
doi_str_mv 10.1021/acsnano.5b04531
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source MEDLINE; American Chemical Society Journals
subjects Chemical Sciences
Gold - chemistry
Material chemistry
Metal Nanoparticles - chemistry
Metal Nanoparticles - ultrastructure
Models, Molecular
Nanotechnology - methods
Proteins - chemistry
title Nanoparticles Self-Assembly Driven by High Affinity Repeat Protein Pairing
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