Nanoparticles Self-Assembly Driven by High Affinity Repeat Protein Pairing
Source abstract
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
References (63)
Show source-provided references
1. 10.1038/nnano.2009.45310.1038/nnano.2009.453 ↗
2. 10.1073/pnas.100114210710.1073/pnas.1001142107 ↗
3. 10.1038/nnano.2013.20910.1038/nnano.2013.209 ↗
4. 10.1038/nmat364710.1038/nmat3647 ↗
5. 10.1038/414735a10.1038/414735a ↗
6. 10.1002/anie.20046214210.1002/anie.200462142 ↗
7. 10.1038/nmat195410.1038/nmat1954 ↗
8. 10.1038/nature1156410.1038/nature11564 ↗
9. 10.1002/anie.20130427310.1002/anie.201304273 ↗
10. 10.1021/nl501581y10.1021/nl501581y ↗
11. 10.1126/science.112036710.1126/science.1120367 ↗
12. 10.1126/science.196221010.1126/science.1962210 ↗
13. 10.1038/nature0140610.1038/nature01406 ↗
14. 10.1039/c4ob00447g10.1039/c4ob00447g ↗
15. 10.1039/b801890a10.1039/b801890a ↗
16. 10.1073/pnas.16210599910.1073/pnas.162105999 ↗
17. 10.1016/j.jmb.2010.09.04810.1016/j.jmb.2010.09.048 ↗
18. 10.1016/j.copbio.2011.06.00410.1016/j.copbio.2011.06.004 ↗
19. 10.1002/anie.20120379510.1002/anie.201203795 ↗
20. 10.1038/nature1340410.1038/nature13404 ↗
21. 10.1039/C4NR01210K10.1039/C4NR01210K ↗
22. 10.1021/ja207898r10.1021/ja207898r ↗
23. 10.1039/b807150k10.1039/b807150k ↗
24. 10.1021/nn200711x10.1021/nn200711x ↗
25. 10.1021/ja805683r10.1021/ja805683r ↗
26. 10.1002/1439-7641(20010316)2:3<184::AID-CPHC184>3.3.CO;2-A10.1002/1439-7641(20010316)2:3<184::AID-CPHC184>3.3.CO;2-A ↗
27. 10.1038/nmat77510.1038/nmat775 ↗
28. 10.1039/b809585j10.1039/b809585j ↗
29. 10.1021/nl034004o10.1021/nl034004o ↗
30. 10.1039/b805874c10.1039/b805874c ↗
31. 10.1002/smll.20050002110.1002/smll.200500021 ↗
32. 10.1002/adma.20050082810.1002/adma.200500828 ↗
33. 10.1021/nl071008a10.1021/nl071008a ↗
34. 10.1038/nphoton.2009.11110.1038/nphoton.2009.111 ↗
35. Dujardin E. · 2010 · 3
36. 10.1021/nl300269c10.1021/nl300269c ↗
37. 10.1021/nl304078v10.1021/nl304078v ↗
38. 10.1126/science.124879710.1126/science.1248797 ↗
39. 10.1039/B514191E10.1039/B514191E ↗
40. 10.1039/c1jm11945a10.1039/c1jm11945a ↗
41. 10.1126/science.119995810.1126/science.1199958 ↗
42. 10.1021/nn303580910.1021/nn3035809 ↗
43. 10.1038/382607a010.1038/382607a0 ↗
44. 10.1038/382609a010.1038/382609a0 ↗
45. 10.1002/(SICI)1521-3773(19980904)37:16<2265::AID-ANIE2265>3.0.CO;2-F10.1002/(SICI)1521-3773(19980904)37:16<2265::AID-ANIE2265>3.0.CO;2-F ↗
46. 10.1002/smll.20040003910.1002/smll.200400039 ↗
47. 10.1038/nmat242110.1038/nmat2421 ↗
48. 10.1038/ncomms791210.1038/ncomms7912 ↗
49. 10.1073/pnas.070080110410.1073/pnas.0700801104 ↗
50. 10.1021/nl203559s10.1021/nl203559s ↗
51. 10.1039/B813429D10.1039/B813429D ↗
52. 10.1002/(SICI)1521-4095(199910)11:14<1202::AID-ADMA1202>3.0.CO;2-H10.1002/(SICI)1521-4095(199910)11:14<1202::AID-ADMA1202>3.0.CO;2-H ↗
53. 10.1021/ja037969i10.1021/ja037969i ↗
54. 10.1021/la000715f10.1021/la000715f ↗
55. 10.1021/nn302546v10.1021/nn302546v ↗
56. 10.1002/(SICI)1521-4095(199904)11:6<449::AID-ADMA449>3.0.CO;2-A10.1002/(SICI)1521-4095(199904)11:6<449::AID-ADMA449>3.0.CO;2-A ↗
57. 10.1371/journal.pone.007151210.1371/journal.pone.0071512 ↗
58. 10.1016/j.jcis.2014.03.00210.1016/j.jcis.2014.03.002 ↗
59. 10.1021/ja902743u10.1021/ja902743u ↗
60. 10.1126/science.112804510.1126/science.1128045 ↗
61. 10.1038/nmat244010.1038/nmat2440 ↗
62. 10.1038/physci241020a010.1038/physci241020a0 ↗
63. 10.1006/abio.1999.440210.1006/abio.1999.4402 ↗