Nanoparticles Self-Assembly Driven by High Affinity Repeat Protein Pairing

被引:55
作者
Gurunatha, Kargal L. [1 ,4 ]
Fournier, Agathe C. [1 ]
Urvoas, Agathe [2 ]
Valerio-Lepiniec, Marie [2 ]
Marchi, Valerie [3 ]
Minard, Philippe [2 ]
Dujardin, Erik [1 ]
机构
[1] CEMES, Grp NanoSci, CNRS, UPR 8011, Rue J Marvig,BP 94347, F-31055 Toulouse, France
[2] Univ Paris 11, I2BC, CNRS, CEA UMR 9198, Bat 430, F-91405 Orsay, France
[3] Univ Rennes 1, Inst Chem Sci, CNRS, UMR 6226, Campus Beaulieu, F-35042 Rennes, France
[4] Univ Calif San Diego, NanoEngn Dept, 9500 Gilman Dr MC 0448, La Jolla, CA 92093 USA
基金
欧洲研究理事会;
关键词
alpha-repeat proteins; gold nanoparticles; reversible self-assembly; protein pair; dissociation constant; GOLD NANOPARTICLES; BUILDING-BLOCKS; INORGANIC NANOPARTICLES; MACROSCOPIC MATERIALS; PLASMON RULER; DNA; NANOSTRUCTURES; TEMPLATES; NANOCRYSTALS; ORGANIZATION;
D O I
10.1021/acsnano.5b04531
中图分类号
O6 [化学];
学科分类号
0703 ;
摘要
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.
引用
收藏
页码:3176 / 3185
页数:10
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