| Literature DB >> 26863288 |
Kargal L Gurunatha1, Agathe C Fournier1, Agathe Urvoas2, Marie Valerio-Lepiniec2, Valérie Marchi3, Philippe Minard2, Erik Dujardin1.
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.Keywords: dissociation constant; gold nanoparticles; protein pair; reversible self-assembly; α-repeat proteins
Mesh:
Substances:
Year: 2016 PMID: 26863288 DOI: 10.1021/acsnano.5b04531
Source DB: PubMed Journal: ACS Nano ISSN: 1936-0851 Impact factor: 15.881