journal article·2025-11

Propagation of Enzyme‐Driven Active Fluctuations in Crowded Milieu

Rik Chakraborty, Diptangshu Paul, Arnab Maiti, K. R. Jayaprakash, Krishna K. Dey

Small· Volume 21· Issue 47
Publisher page

Abstract

Abstract The recently observed capability of active enzyme molecules to transduce mechanical energy during catalytic turnover and thereby influence the dynamics of their surroundings, akin to the adenosine triphosphate (ATP)‐driven molecular motors, has opened up new research avenues in molecular biophysics. In this study, the energy transfer from active enzymes to their surroundings in crowded environments is investigated by measuring the diffusion of passive microscopic tracers in active solutions of ficoll and glycerol. Despite observing lower rates of substrate turnover, a significantly higher relative enhancement of passive tracer diffusion is found in crowded environments compared to those in aqueous solutions in the presence of enzymatic activity. The experimental observations, coupled with supporting theoretical estimations, underscore the possible role of the intervening media in facilitating mechanical energy distribution around active enzymes, which might have important implications over various biochemical processes in active intracellular milieu.
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Research context

OpenAlex topics: Micro and Nano Robotics · Lipid Membrane Structure and Behavior · Hemoglobin structure and function

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

Affiliations

Laboratory of Soft and Living Materials Department of Physics Indian Institute of Technology Gandhinagar Gandhinagar Gujarat 382055 India

Department of Mechanical Engineering Indian Institute of Technology Gandhinagar Gandhinagar Gujarat 382055 India

Funding

Ministry of Education, India

References (62)

Show source-provided references
1. 10.7566/JPSJ.92.05480110.7566/JPSJ.92.054801 ↗
2. 10.1146/annurev-conmatphys-061020-05303610.1146/annurev-conmatphys-061020-053036 ↗
3. 10.1146/annurev-biophys-121219-08153510.1146/annurev-biophys-121219-081535 ↗
4. 10.1021/acscentsci.9b0022810.1021/acscentsci.9b00228 ↗
5. Jee A.‐Y. · Proc. Natl. Acad. Sci. U.S.A. · 2018 · 115
6. 10.1021/nn507039b10.1021/nn507039b ↗
7. 10.1021/ja908773a10.1021/ja908773a ↗
8. 10.1038/nature1404310.1038/nature14043 ↗
9. 10.1073/pnas.201981011710.1073/pnas.2019810117 ↗
10. 10.1103/PhysRevLett.123.12810110.1103/PhysRevLett.123.128101 ↗
11. 10.1039/C9CP02842K10.1039/C9CP02842K ↗
12. 10.1039/D2SM00054G10.1039/D2SM00054G ↗
13. 10.1016/j.bpj.2018.02.00810.1016/j.bpj.2018.02.008 ↗
14. 10.1209/0295-5075/119/4000210.1209/0295-5075/119/40002 ↗
15. 10.1119/1.1090310.1119/1.10903 ↗
16. 10.1063/1.493342410.1063/1.4933424 ↗
17. 10.1021/acs.accounts.8b0027610.1021/acs.accounts.8b00276 ↗
18. 10.1021/acs.nanolett.8b0424010.1021/acs.nanolett.8b04240 ↗
19. 10.1021/jacs.9b0694910.1021/jacs.9b06949 ↗
20. 10.1073/pnas.200690011710.1073/pnas.2006900117 ↗
21. 10.1021/jacs.1c1232810.1021/jacs.1c12328 ↗
22. 10.1073/pnas.150682511210.1073/pnas.1506825112 ↗
23. 10.1016/j.physd.2015.10.02410.1016/j.physd.2015.10.024 ↗
24. 10.1039/C7SM00400A10.1039/C7SM00400A ↗
25. 10.1209/0295-5075/128/4000310.1209/0295-5075/128/40003 ↗
26. 10.1038/s42005-022-00878-310.1038/s42005-022-00878-3 ↗
27. 10.1039/D0SM01138J10.1039/D0SM01138J ↗
28. 10.1021/acs.nanolett.7b0161810.1021/acs.nanolett.7b01618 ↗
29. 10.1002/anie.20180459910.1002/anie.201804599 ↗
30. 10.1021/acs.analchem.2c0036310.1021/acs.analchem.2c00363 ↗
31. 10.1103/PhysRevE.109.05460710.1103/PhysRevE.109.054607 ↗
32. 10.1083/jcb.20080614910.1083/jcb.200806149 ↗
33. 10.1016/j.cell.2014.06.05110.1016/j.cell.2014.06.051 ↗
34. 10.1126/science.116937510.1126/science.1169375 ↗
35. 10.1371/journal.pone.009170010.1371/journal.pone.0091700 ↗
36. 10.1016/j.jtbi.2020.11037010.1016/j.jtbi.2020.110370 ↗
37. 10.1073/pnas.110728110910.1073/pnas.1107281109 ↗
38. 10.1371/journal.pone.002870710.1371/journal.pone.0028707 ↗
39. 10.1021/acs.jpcb.9b0123910.1021/acs.jpcb.9b01239 ↗
40. 10.1063/1.347307010.1063/1.3473070 ↗
41. 10.1103/PhysRevLett.124.18800110.1103/PhysRevLett.124.188001 ↗
42. 10.1006/abbi.1997.991010.1006/abbi.1997.9910 ↗
43. 10.1038/s41598-020-69638-z10.1038/s41598-020-69638-z ↗
44. 10.1016/j.bbapap.2021.14069910.1016/j.bbapap.2021.140699 ↗
45. 10.1021/acs.biochem.6b0005310.1021/acs.biochem.6b00053 ↗
46. 10.1016/j.bbagen.2016.11.01410.1016/j.bbagen.2016.11.014 ↗
47. 10.1103/PhysRevE.49.515810.1103/PhysRevE.49.5158 ↗
48. 10.1103/PhysRevLett.115.10810210.1103/PhysRevLett.115.108102 ↗
49. 10.1007/s12195-014-0376-110.1007/s12195-014-0376-1 ↗
50. 10.1039/C8CC02426J10.1039/C8CC02426J ↗
51. 10.1016/S0041-624X(02)00372-410.1016/S0041-624X(02)00372-4 ↗
52. 10.1121/10.000499910.1121/10.0004999 ↗
53. Temkin S. · 1981
54. 10.1021/jp501583t10.1021/jp501583t ↗
55. 10.1007/s00348-018-2527-y10.1007/s00348-018-2527-y ↗
56. 10.1002/slct.20230157010.1002/slct.202301570 ↗
57. 10.1103/PhysRevApplied.11.02401810.1103/PhysRevApplied.11.024018 ↗
58. 10.1103/PhysRevE.94.02241610.1103/PhysRevE.94.022416 ↗
59. 10.1103/PhysRevE.95.03241710.1103/PhysRevE.95.032417 ↗
60. 10.1103/PhysRevE.108.05460610.1103/PhysRevE.108.054606 ↗
61. 10.1016/j.cell.2013.11.02810.1016/j.cell.2013.11.028 ↗
62. 10.1006/jcis.1996.021710.1006/jcis.1996.0217 ↗