journal article·2016-03-22Open access

Nanoparticles Self-Assembly Driven by High Affinity Repeat Protein Pairing

Kargal L. Gurunatha, Agathe C. Fournier, Agathe Urvoas, Marie Valerio-Lepiniec, Valérie Marchi, Philippe Minard, Erik Dujardin

ACS Nano· Volume 10· Issue 3

Abstract

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 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.
Source: openalex_inverted_index · Quality: baseline

Research context

OpenAlex topics: Nanocluster Synthesis and Applications · Quantum Dots Synthesis And Properties · Bacteriophages and microbial interactions

SciVX discovery tags are terminology-based. OpenAlex topics are source-provided classifications.

Affiliations

Groupe NanoSciences-CEMES, CNRS UPR 8011, 29 rue J. Marvig, B.P. 94347, F-31055 Toulouse, France

I2BC, Univ Paris Sud, CNRS, CEA UMR 9198, Bât. 430, F-91405 Orsay, France

University Rennes 1, Institut of Chemical Sciences, UMR 6226 CNRS, Campus Beaulieu, F- 35042 Rennes, France

Funding

Agence Nationale de la Recherche · European Research Council · Centre National de la Recherche Scientifique

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