Photo-Fenozyme Nanoparticles Based on Fe(II)-Coordination-Driven Cyanine-Based Amino Acid Assembly for Photodynamic Ferrotherapy
Source abstract
Abstract
Nanoparticle-based enzyme mimics have fewer applications in ferrotherapy so far. The limited number of integrated biomimetic architectures satisfy biobuilding blocks and adaptability in the high efficiency of ferrotherapy requirements. Herein, we develop a minimal nanoparticle as an efficient photodynamic ferrotherapy agent, which is constructed through ferrous-coordination-driven cyanine-based amino acid assembly. In comparison with a free photosensitizer, this nanoparticle (photofenozyme) composed of Fe-containing cores and serum protein shells is fabricated. And it has a high light-harvesting ability, and a higher intersystem crossing (ISC) rate constant (4.41 × 1011 s–1 versus 1.17 × 106 s–1), which benefits efficient production of the triplet state. The photofenozyme allows adaptive photo-Fenton-like activity based on the different radical generations. And they further trigger and photoenhance efficient ferroptosis. This work provides insights into optimizing current photosensitizers to generate an adaptive supramolecular photocatalyst and presents a promising strategy to design multifunctional nanozyme theranostics.
Source: openalex_inverted_index · Quality: baseline
Research context
OpenAlex topics: Advanced Nanomaterials in Catalysis · Nanoplatforms for cancer theranostics · Advanced Photocatalysis Techniques
SciVX discovery tags are terminology-based. OpenAlex topics are source-provided classifications.
Affiliations
Department of Chemistry and Nanoscience, Ewha Womans University, Seoul 03760, Republic of Korea
Department of Chemistry, Korea University, Seoul 02841, Republic of Korea
College of Chemistry, State Key Laboratory of Photocatalysis on Energy and Environment, Fujian Provincial Key Laboratory of Cancer Metastasis Chemoprevention and Chemotherapy, Fuzhou University, Fuzhou 350108, P. R. China
Funding
National Research Foundation of Korea
References (65)
Show source-provided references
1. 10.1038/s41589-020-0472-610.1038/s41589-020-0472-6 ↗
2. 10.1038/s41467-017-00424-810.1038/s41467-017-00424-8 ↗
3. 10.1126/science.aah442710.1126/science.aah4427 ↗
4. 10.1021/acscatal.0c0375310.1021/acscatal.0c03753 ↗
5. 10.1039/C7CS00471K10.1039/C7CS00471K ↗
6. 10.1038/s41467-020-15730-x10.1038/s41467-020-15730-x ↗
7. 10.1021/acsnano.9b0778910.1021/acsnano.9b07789 ↗
8. 10.1021/acscatal.8b0332610.1021/acscatal.8b03326 ↗
9. 10.1021/acscatal.0c0164710.1021/acscatal.0c01647 ↗
10. 10.1021/acsabm.0c0112710.1021/acsabm.0c01127 ↗
11. 10.1039/a804252g10.1039/a804252g ↗
12. 10.1039/C9NR10822J10.1039/C9NR10822J ↗
13. 10.1021/acsami.8b1531810.1021/acsami.8b15318 ↗
14. 10.1039/D0NR02800B10.1039/D0NR02800B ↗
15. 10.1038/s41467-019-14199-710.1038/s41467-019-14199-7 ↗
16. 10.1093/jnci/90.12.88910.1093/jnci/90.12.889 ↗
17. 10.1002/anie.20180655110.1002/anie.201806551 ↗
18. 10.1021/acsnano.7b0774610.1021/acsnano.7b07746 ↗
19. 10.1016/j.cbi.2005.12.00910.1016/j.cbi.2005.12.009 ↗
20. 10.1002/anie.19960706110.1002/anie.199607061 ↗
21. 10.1002/anie.20181147810.1002/anie.201811478 ↗
22. 10.1126/science.115269210.1126/science.1152692 ↗
23. 10.1126/science.270.5238.93510.1126/science.270.5238.935 ↗
24. 10.1038/nature1111710.1038/nature11117 ↗
25. 10.1038/nchem.74410.1038/nchem.744 ↗
26. 10.1021/jacs.8b0755310.1021/jacs.8b07553 ↗
27. 10.1016/j.cej.2020.12498710.1016/j.cej.2020.124987 ↗
28. 10.1002/anie.20100038010.1002/anie.201000380 ↗
29. 10.1021/ja060399c10.1021/ja060399c ↗
30. 10.1016/S1010-6030(03)00203-X10.1016/S1010-6030(03)00203-X ↗
31. 10.1016/j.biomaterials.2013.05.07110.1016/j.biomaterials.2013.05.071 ↗
32. 10.1021/acsnano.8b0352910.1021/acsnano.8b03529 ↗
33. 10.1002/ange.20201000510.1002/ange.202010005 ↗
34. 10.1021/acsnano.9b0344410.1021/acsnano.9b03444 ↗
35. 10.1126/science.125.3243.353-a10.1126/science.125.3243.353-a ↗
36. 10.1002/anie.20170535710.1002/anie.201705357 ↗
37. 10.1016/j.chempr.2018.06.00310.1016/j.chempr.2018.06.003 ↗
38. Hauser A. · 2004 · 15510.1007/b95416 ↗
39. 10.1007/BF0003713110.1007/BF00037131 ↗
40. 10.1126/science.109016510.1126/science.1090165 ↗
41. 10.1021/ja00257a04210.1021/ja00257a042 ↗
42. 10.1016/j.biomaterials.2012.07.01410.1016/j.biomaterials.2012.07.014 ↗
43. 10.1016/j.freeradbiomed.2011.05.03910.1016/j.freeradbiomed.2011.05.039 ↗
44. 10.1021/ja00796a01110.1021/ja00796a011 ↗
45. 10.1021/jacs.8b0491210.1021/jacs.8b04912 ↗
46. 10.1021/jacs.6b0794610.1021/jacs.6b07946 ↗
47. 10.1016/0006-2952(83)90052-710.1016/0006-2952(83)90052-7 ↗
48. 10.1039/c2sc20540h10.1039/c2sc20540h ↗
49. 10.1016/j.bbabio.2012.09.00710.1016/j.bbabio.2012.09.007 ↗
50. 10.1039/C5SC01733E10.1039/C5SC01733E ↗
51. Ubiquitous Roles of Cytochrome P450 Proteins · 27
52. 10.1021/acsnano.0c0062910.1021/acsnano.0c00629 ↗
53. 10.1002/smll.20190532610.1002/smll.201905326 ↗
54. 10.1038/nchembio.155510.1038/nchembio.1555 ↗
55. 10.1002/anie.20060258110.1002/anie.200602581 ↗
56. 10.1074/jbc.M30005420010.1074/jbc.M300054200 ↗
57. 10.1074/jbc.M41166220010.1074/jbc.M411662200 ↗
58. 10.1016/0891-5849(94)90127-910.1016/0891-5849(94)90127-9 ↗
59. 10.1016/j.jphotobiol.2020.11178710.1016/j.jphotobiol.2020.111787 ↗
60. 10.1002/anie.20170096810.1002/anie.201700968 ↗
61. 10.7150/thno.4188210.7150/thno.41882 ↗
62. 10.1016/j.cell.2012.03.04210.1016/j.cell.2012.03.042 ↗
63. 10.1021/acsnano.1c0124810.1021/acsnano.1c01248 ↗
64. 10.1002/adfm.20200064710.1002/adfm.202000647 ↗
65. 10.1021/acs.nanolett.9b0377410.1021/acs.nanolett.9b03774 ↗