DataVXChemNanoMatPaper
journal article·2020-01

Unsaturation‐Dependent Nanostructures Self‐Assembled from Oligopeptide Amphiphiles Capable of Generating Singlet Oxygen

Jia‐Ru Feng, Si‐Yong Qin, Lei Rong, Yin‐Jia Cheng, Yi‐Han Ma, Ai‐Qing Zhang

ChemNanoMat· Volume 6· Issue 1
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Source abstract

Abstract

Abstract We report here on three oligopeptide amphiphiles (OPA1‐3) with different unsaturated double bonds, which self‐assemble into shape‐specific nanostructures. It was found that OPA1 with saturated hydrophobic tail self‐assembled into conventional cylindrical nanofibers, while the unsaturated OPA2‐3 molecules self‐organized into helical nanoarchitectures. Due to the different double bond numbers in hydrophobic tails of OPA2‐3, the helical pitch and width of their self‐assemblies varied. Specially, linoleic acid‐bearing OPA3 could be oxidized by lipoxidase to create hydroperoxide‐containing OPA4, which further generated singlet oxygen (1O2) in the presence of catalytic iron (II) ion. The established system may provide a self‐deliverable nanoplatform for 1O2‐mediated cancer treatment.
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Research context

NanomaterialsCatalysis & surfaces

OpenAlex topics: Nanoplatforms for cancer theranostics · Supramolecular Self-Assembly in Materials · Luminescence and Fluorescent Materials

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

Affiliations

Key Laboratory of Catalysis and Energy Materials Chemistry of Ministry of Education & Hubei Key Laboratory of Catalysis and Materials Science South-Central University for Nationalities Wuhan 430074 P. R. China

State Key Laboratory of Natural Medicines and Jiangsu Key Laboratory of Drug Discovery for Metabolic Diseases Center of Advanced Pharmaceuticals and Biomaterials China Pharmaceutical University Nanjing 210009 P. R. China

Funding

National Natural Science Foundation of China · Fundamental Research Funds for the Central Universities

References (28)

Show source-provided references
1. 10.1039/C5CC00501A10.1039/C5CC00501A ↗
2. 10.1021/acsnano.8b0380010.1021/acsnano.8b03800 ↗
3. 10.1002/adma.20160406210.1002/adma.201604062 ↗
4. 10.1039/C8RA06034G10.1039/C8RA06034G ↗
5. 10.1038/nnano.2015.31210.1038/nnano.2015.312 ↗
6. 10.1039/C2TB00105E10.1039/C2TB00105E ↗
7. 10.1021/acs.chemmater.8b0349610.1021/acs.chemmater.8b03496 ↗
8. 10.7150/thno.1542010.7150/thno.15420 ↗
9. 10.1021/jacs.6b1138210.1021/jacs.6b11382 ↗
10. 10.1021/jacs.7b1236810.1021/jacs.7b12368 ↗
11. 10.1039/C8CC09548E10.1039/C8CC09548E ↗
12. 10.1039/C5NR03862F10.1039/C5NR03862F ↗
13. 10.1021/acs.accounts.7b0029710.1021/acs.accounts.7b00297 ↗
14. Silva G. A. · Science · 2004 · 10
15. 10.1007/s12274-015-0945-110.1007/s12274-015-0945-1 ↗
16. 10.1016/j.colsurfb.2010.07.02710.1016/j.colsurfb.2010.07.027 ↗
17. 10.1021/la501298810.1021/la5012988 ↗
18. 10.1021/jacs.8b0932010.1021/jacs.8b09320 ↗
19. 10.1016/j.colsurfb.2018.02.05410.1016/j.colsurfb.2018.02.054 ↗
20. 10.1002/anie.20170118110.1002/anie.201701181 ↗
21. 10.1021/ja020752o10.1021/ja020752o ↗
22. 10.1002/chem.20100304910.1002/chem.201003049 ↗
23. 10.1002/smll.20170217510.1002/smll.201702175 ↗
24. 10.1002/marc.20110005210.1002/marc.201100052 ↗
25. 10.1039/c3sm52730a10.1039/c3sm52730a ↗
26. 10.1016/j.biomaterials.2018.10.00510.1016/j.biomaterials.2018.10.005 ↗
27. 10.1021/acs.chemrev.8b0062610.1021/acs.chemrev.8b00626 ↗
28. 10.1021/ar600050710.1021/ar6000507 ↗