journal article·2022-04Open access

History Dependence in a Chemical Reaction Network Enables Dynamic Switching

Dmitrii V. Kriukov, A. Hazal Koyuncu, Albert S. Y. Wong

Small· Volume 18· Issue 16

Abstract

Abstract This work describes an enzymatic autocatalytic network capable of dynamic switching under out‐of‐equilibrium conditions. The network, wherein a molecular fuel (trypsinogen) and an inhibitor (soybean trypsin inhibitor) compete for a catalyst (trypsin), is kept from reaching equilibria using a continuous flow stirred tank reactor. A so‐called ‘linear inhibition sweep’ is developed (i.e., a molecular analogue of linear sweep voltammetry) to intentionally perturb the competition between autocatalysis and inhibition, and used to demonstrate that a simple molecular system, comprising only three components, is already capable of a variety of essential neuromorphic behaviors (hysteresis, synchronization, resonance, and adaptation). This research provides the first steps in the development of a strategy that uses the principles in systems chemistry to transform chemical reaction networks into platforms capable of neural network computing.
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Research context

OpenAlex topics: Photoreceptor and optogenetics research · Gene Regulatory Network Analysis · Neural dynamics and brain function

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

Affiliations

Department of Molecules and Materials Faculty of Science and Technology University of Twente Drienerlolaan 5 Enschede 7522 NH The Netherlands

MESA+ Institute for Nanotechnology University of Twente Drienerlolaan 5 Enschede 7522 NH The Netherlands

BRAINS (Center for Brain‐inspired Nano Systems) University of Twente Drienerlolaan 5 Enschede 7522 NH The Netherlands

References (43)

Show source-provided references
1. 10.1109/JPROC.2017.276174010.1109/JPROC.2017.2761740 ↗
2. 10.1038/d41586-018-06610-y10.1038/d41586-018-06610-y ↗
3. 10.1038/s41586-021-03453-y10.1038/s41586-021-03453-y ↗
4. 10.1038/nature1026210.1038/nature10262 ↗
5. 10.1038/s41586-018-0289-610.1038/s41586-018-0289-6 ↗
6. 10.1038/s41467-020-15190-310.1038/s41467-020-15190-3 ↗
7. 10.1038/s41586-021-03748-010.1038/s41586-021-03748-0 ↗
8. 10.1126/science.285.5426.39110.1126/science.285.5426.391 ↗
9. 10.1038/3503608610.1038/35036086 ↗
10. 10.1142/S021812740802175010.1142/S0218127408021750 ↗
11. 10.3762/bjnano.5.12310.3762/bjnano.5.123 ↗
12. 10.1038/nrm253010.1038/nrm2530 ↗
13. 10.1016/S0955-0674(03)00017-610.1016/S0955-0674(03)00017-6 ↗
14. 10.1038/nrg127210.1038/nrg1272 ↗
15. 10.1126/science.298.5594.82410.1126/science.298.5594.824 ↗
16. 10.1039/C7CS90088K10.1039/C7CS90088K ↗
17. 10.1007/978-3-030-03858-810.1007/978-3-030-03858-8 ↗
18. 10.1137/05063417710.1137/050634177 ↗
19. 10.1126/science.118337210.1126/science.1183372 ↗
20. 10.1038/nature1977610.1038/nature19776 ↗
21. 10.1038/nchem.214210.1038/nchem.2142 ↗
22. 10.1126/science.aac610310.1126/science.aac6103 ↗
23. 10.1126/science.118276710.1126/science.1182767 ↗
24. 10.1039/C6CS00738D10.1039/C6CS00738D ↗
25. 10.1109/PROC.1976.1009210.1109/PROC.1976.10092 ↗
26. 10.1002/adma.20190276110.1002/adma.201902761 ↗
27. 10.1016/j.tet.2017.04.05310.1016/j.tet.2017.04.053 ↗
28. 10.1016/j.tibs.2014.10.00210.1016/j.tibs.2014.10.002 ↗
29. 10.1021/jp953547m10.1021/jp953547m ↗
30. 10.1038/376307a010.1038/376307a0 ↗
31. 10.1038/nrm183810.1038/nrm1838 ↗
32. 10.1016/j.cell.2013.02.00510.1016/j.cell.2013.02.005 ↗
33. 10.1021/bi00429a02210.1021/bi00429a022 ↗
34. 10.1016/S1369-7021(08)70119-610.1016/S1369-7021(08)70119-6 ↗
35. 10.1103/RevModPhys.70.22310.1103/RevModPhys.70.223 ↗
36. Perunov N. · Phys. Rev. X · 2016 · 6 · 021036
37. 10.1038/nnano.2016.11610.1038/nnano.2016.116 ↗
38. 10.1039/C2LC40649G10.1039/C2LC40649G ↗
39. 10.1038/nnano.2016.29910.1038/nnano.2016.299 ↗
40. 10.1002/smll.20200716610.1002/smll.202007166 ↗
41. 10.1002/anie.20190799510.1002/anie.201907995 ↗
42. 10.1039/D0SC05860B10.1039/D0SC05860B ↗
43. 10.1073/pnas.201352711710.1073/pnas.2013527117 ↗