journal article·2019-04-23Open access

Synthetically Diversified Protein Nanopores: Resolving Click Reaction Mechanisms

Marius M. Haugland, Stefan Borsley, Dominic F. Cairns-Gibson, Alex Elmi, Scott L. Cockroft

ACS Nano· Volume 13· Issue 4

Abstract

Nanopores are emerging as a powerful tool for the investigation of nanoscale processes at the single-molecule level. Here, we demonstrate the methionine-selective synthetic diversification of α-hemolysin (α-HL) protein nanopores and their exploitation as a platform for investigating reaction mechanisms. A wide range of functionalities, including azides, alkynes, nucleotides, and single-stranded DNA, were incorporated into individual pores in a divergent fashion. The ion currents flowing through the modified pores were used to observe the trajectory of a range of azide-alkyne click reactions and revealed several short-lived intermediates in Cu(I)-catalyzed azide-alkyne [3 + 2] cycloadditions (CuAAC) at the single-molecule level. Analysis of ion-current fluctuations enabled the populations of species involved in rapidly exchanging equilibria to be determined, facilitating the resolution of several transient intermediates in the CuAAC reaction mechanism. The versatile pore-modification chemistry offers a useful approach for enabling future physical organic investigations of reaction mechanisms at the single-molecule level.
Source: openalex_inverted_index · Quality: baseline

Research context

OpenAlex topics: Nanopore and Nanochannel Transport Studies · Advanced biosensing and bioanalysis techniques · RNA Interference and Gene Delivery

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

Affiliations

EaStCHEM School of Chemistry, University of Edinburgh, Joseph Black Building, David Brewster Road, Edinburgh EH9 3FJ, United Kingdom

Funding

FP7 Ideas: European Research Council

References (58)

Show source-provided references
1. 10.1038/3509303810.1038/35093038 ↗
2. 10.1039/b414551h10.1039/b414551h ↗
3. 10.1002/chem.20180066910.1002/chem.201800669 ↗
4. 10.1021/acs.accounts.7b0014310.1021/acs.accounts.7b00143 ↗
5. 10.1038/nnano.2007.2710.1038/nnano.2007.27 ↗
6. Tagliazucchi, M. In Chemically Modified Nanopores and Nanochannels; Tagliazucchi, M., Szleifer, I., Eds. William Andrew Publishing: Boston, 2017; p 1–25.10.1016/B978-0-323-40182-1.00001-4 ↗
7. 10.1038/nnano.2017.9910.1038/nnano.2017.99 ↗
8. 10.1039/C7SC01940H10.1039/C7SC01940H ↗
9. 10.1002/anie.20171274010.1002/anie.201712740 ↗
10. 10.1021/jacs.6b1228410.1021/jacs.6b12284 ↗
11. 10.1021/jacs.5b1071010.1021/jacs.5b10710 ↗
12. 10.1002/chem.20180076010.1002/chem.201800760 ↗
13. 10.1038/srep0166210.1038/srep01662 ↗
14. 10.1002/anie.20100546010.1002/anie.201005460 ↗
15. 10.1039/C7CC04599A10.1039/C7CC04599A ↗
16. 10.1021/ja800460710.1021/ja8004607 ↗
17. 10.1038/nchem.194910.1038/nchem.1949 ↗
18. 10.1073/pnas.151056511210.1073/pnas.1510565112 ↗
19. 10.1021/acsnano.6b0466310.1021/acsnano.6b04663 ↗
20. 10.1002/anie.20171026210.1002/anie.201710262 ↗
21. 10.1002/anie.20070073610.1002/anie.200700736 ↗
22. 10.1021/jacs.8b0059310.1021/jacs.8b00593 ↗
23. 10.1021/acsnano.6b0599510.1021/acsnano.6b05995 ↗
24. 10.1002/anie.20150884510.1002/anie.201508845 ↗
25. 10.1039/C5CS00874C10.1039/C5CS00874C ↗
26. 10.1126/science.aat387210.1126/science.aat3872 ↗
27. 10.1039/C2CS35286A10.1039/C2CS35286A ↗
28. 10.1021/nn305167710.1021/nn3051677 ↗
29. 10.1021/nl070462b10.1021/nl070462b ↗
30. 10.1021/nn301011910.1021/nn3010119 ↗
31. 10.1021/ja076184010.1021/ja0761840 ↗
32. 10.1021/nl103887410.1021/nl1038874 ↗
33. 10.1126/science.274.5294.185910.1126/science.274.5294.1859 ↗
34. 10.1021/acsnano.7b0810510.1021/acsnano.7b08105 ↗
35. 10.1126/science.aal331610.1126/science.aal3316 ↗
36. 10.1021/nl401968r10.1021/nl401968r ↗
37. 10.1007/7081_2011_7210.1007/7081_2011_72 ↗
38. 10.1021/acs.bioconjchem.7b0063310.1021/acs.bioconjchem.7b00633 ↗
39. 10.3390/molecules2110139310.3390/molecules21101393 ↗
40. 10.1002/anie.20090548310.1002/anie.200905483 ↗
41. 10.1038/nbt.342310.1038/nbt.3423 ↗
42. 10.1373/clinchem.2014.22301610.1373/clinchem.2014.223016 ↗
43. 10.1126/sciadv.150030410.1126/sciadv.1500304 ↗
44. 10.1039/C7RA10653J10.1039/C7RA10653J ↗
45. 10.1002/tcr.20160000210.1002/tcr.201600002 ↗
46. 10.1126/science.122950610.1126/science.1229506 ↗
47. 10.1002/anie.20046149610.1002/anie.200461496 ↗
48. 10.1021/om700669v10.1021/om700669v ↗
49. 10.1021/ja203733q10.1021/ja203733q ↗
50. 10.1021/ja047152510.1021/ja0471525 ↗
51. 10.3762/bjoc.9.30810.3762/bjoc.9.308 ↗
52. 10.1002/anie.20141030110.1002/anie.201410301 ↗
53. 10.1039/C8CS00354H10.1039/C8CS00354H ↗
54. 10.1038/nchem.265110.1038/nchem.2651 ↗
55. 10.1038/s41929-018-0109-210.1038/s41929-018-0109-2 ↗
56. 10.1021/jacs.8b0823310.1021/jacs.8b08233 ↗
57. 10.1021/jacs.8b0019210.1021/jacs.8b00192 ↗
58. 10.1039/C8CS00352A10.1039/C8CS00352A ↗