Scaffolding of Enzymes on Virus Nanoarrays: Effects of Confinement and Virus Organization on Biocatalysis
Source abstract
Abstract
Organizing active enzyme molecules on nanometer‐sized scaffolds is a promising strategy for designing highly efficient supported catalytic systems for biosynthetic and sensing applications. This is achieved by designing model nanoscale enzymatic platforms followed by thorough analysis of the catalytic activity. Herein, the virus fd bacteriophage is considered as an enzyme nanocarrier to study the scaffolding effects on enzymatic activity. Nanoarrays of randomly oriented, or directionally patterned, fd bacteriophage virus are functionalized with the enzyme glucose oxidase (GOx), using an immunological assembly strategy, directly on a gold electrode support. The scaffolding process on the virus capsid is monitored in situ by AFM (atomic force microscopy) imaging, while cyclic voltammetry is used to interrogate the catalytic activity of the resulting functional GOx‐fd nanoarrays. Kinetic analysis reveals the ability to modulate the activity of GOx via nanocarrier patterning. The results evidence, for the first time, enhancement of the enzymatic activity due to scaffolding on a filamentous viral particle.
Source: crossref · Quality: baseline
Research context
OpenAlex topics: Advanced biosensing and bioanalysis techniques · Bacteriophages and microbial interactions · Monoclonal and Polyclonal Antibodies Research
SciVX discovery tags are terminology-based. OpenAlex topics are source-provided classifications.
Affiliations
Laboratoire d'Electrochimie Moléculaire UMR 7591 CNRS Université Paris Diderot Sorbonne Paris Cité 15 rue Jean‐Antoine de Baïf F‐75205 Paris Cedex 13 France
Centre de Recherche Paul‐Pascal UPR 8641 CNRS Université de Bordeaux 115 avenue Schweitzer 33600 Pessac France
Biologie du Fruit et Pathologie UMR 1332 INRA Université de Bordeaux 71 avenue Edouard Bourlaux, CS20032 33882 Villenave d'Ornon Cedex France
Funding
Agence Nationale de la Recherche
References (63)
Show source-provided references
1. 10.1016/j.pbi.2005.03.01410.1016/j.pbi.2005.03.014 ↗
2. 10.1016/j.copbio.2008.07.00610.1016/j.copbio.2008.07.006 ↗
3. 10.1021/acs.chemrev.5b0034410.1021/acs.chemrev.5b00344 ↗
4. 10.1016/j.copbio.2013.11.00710.1016/j.copbio.2013.11.007 ↗
5. Michon T. · 2016
6. 10.1016/j.tibtech.2012.04.00110.1016/j.tibtech.2012.04.001 ↗
7. 10.1002/smll.20130139310.1002/smll.201301393 ↗
8. 10.1021/ja300897h10.1021/ja300897h ↗
9. 10.1021/jacs.5b1019810.1021/jacs.5b10198 ↗
10. 10.1021/cb400652910.1021/cb4006529 ↗
11. 10.3389/fpls.2015.0113710.3389/fpls.2015.01137 ↗
12. 10.3389/fpls.2016.0008910.3389/fpls.2016.00089 ↗
13. 10.1016/j.copbio.2013.01.00310.1016/j.copbio.2013.01.003 ↗
14. 10.1021/cs401009z10.1021/cs401009z ↗
15. 10.1016/j.nantod.2014.02.00510.1016/j.nantod.2014.02.005 ↗
16. 10.1002/smll.20130363910.1002/smll.201303639 ↗
17. 10.1016/j.copbio.2015.04.00510.1016/j.copbio.2015.04.005 ↗
18. Rurup W. F. · 2016
19. 10.1038/nnano.2007.29910.1038/nnano.2007.299 ↗
20. 10.1038/nnano.2007.7610.1038/nnano.2007.76 ↗
21. 10.1002/anie.20100524310.1002/anie.201005243 ↗
22. 10.1039/C0SC00407C10.1039/C0SC00407C ↗
23. 10.1039/c2nr31485a10.1039/c2nr31485a ↗
24. 10.1021/nn300545z10.1021/nn300545z ↗
25. 10.1021/nn302183h10.1021/nn302183h ↗
26. 10.1039/c2sm26485d10.1039/c2sm26485d ↗
27. 10.1021/bm401291u10.1021/bm401291u ↗
28. 10.1021/acsnano.5b0458010.1021/acsnano.5b04580 ↗
29. Cerf A. · 2016
30. 10.1002/anie.20050197810.1002/anie.200501978 ↗
31. 10.1002/smll.20100086310.1002/smll.201000863 ↗
32. 10.1002/anie.20100465410.1002/anie.201004654 ↗
33. 10.1073/pnas.22145829810.1073/pnas.221458298 ↗
34. 10.1016/j.bios.2011.12.01910.1016/j.bios.2011.12.019 ↗
35. 10.1016/j.colsurfb.2014.05.03610.1016/j.colsurfb.2014.05.036 ↗
36. 10.1016/j.jelechem.2016.05.01910.1016/j.jelechem.2016.05.019 ↗
37. 10.1016/S0021-9258(17)35990-210.1016/S0021-9258(17)35990-2 ↗
38. 10.1016/S0021-9258(18)91224-X10.1016/S0021-9258(18)91224-X ↗
39. 10.1016/S0021-9258(18)62246-X10.1016/S0021-9258(18)62246-X ↗
40. 10.1016/j.jbiotec.2010.10.07710.1016/j.jbiotec.2010.10.077 ↗
41. 10.1021/ja00054a00110.1021/ja00054a001 ↗
42. 10.1021/ja00079a00510.1021/ja00079a005 ↗
43. 10.1021/acsnano.5b0095210.1021/acsnano.5b00952 ↗
44. 10.1128/aem.49.1.91-95.198510.1128/aem.49.1.91-95.1985 ↗
45. 10.1093/nar/21.5.111710.1093/nar/21.5.1117 ↗
46. 10.1038/nmat159610.1038/nmat1596 ↗
47. 10.1002/bit.2201710.1002/bit.22017 ↗
48. 10.1128/MMBR.00041-1010.1128/MMBR.00041-10 ↗
49. 10.1021/ac020385z10.1021/ac020385z ↗
50. 10.1016/S0021-9258(18)97448-X10.1016/S0021-9258(18)97448-X ↗
51. 10.1021/bc300130z10.1021/bc300130z ↗
52. 10.1016/j.snb.2016.07.09610.1016/j.snb.2016.07.096 ↗
53. 10.1002/adma.20130586210.1002/adma.201305862 ↗
54. 10.1063/1.354911310.1063/1.3549113 ↗
55. 10.1021/la502534t10.1021/la502534t ↗
56. 10.1039/C2TB00066K10.1039/C2TB00066K ↗
57. 10.1126/science.752234710.1126/science.7522347 ↗
58. 10.1021/la800224s10.1021/la800224s ↗
59. 10.1002/chem.20080068110.1002/chem.200800681 ↗
60. 10.1021/ja207123710.1021/ja2071237 ↗
61. 10.1021/ac400180510.1021/ac4001805 ↗
62. Sambrook J. · 1989
63. 10.1021/nn400527u10.1021/nn400527u ↗