Facile Synthesis of Peptide Cross-Linked Nanogels for Tumor Metastasis Inhibition
Source abstract
Abstract
Cancer metastasis is one of the major factors contributing to high mortality, and here we designed and synthesized a peptide cross-linked nanogel for hydrophilic functional molecule encapsulation and tumor metastasis inhibition. In this investigation, matrix metalloproteinase-2 (MMP2)-responsive peptide cross-linker is prepared by coupling acrylate-functional groups at both peptide terminals. The peptide cross-linked nanogel is then synthesized by free radical precipitation polymerization using N -isopropylacrylamide as the scaffold. Meanwhile, the hydrophilic tumor metastasis inhibition peptide P-5m is encapsulated into the nanogel in the one-pot synthesis step without complex cooperation. Importantly, the size-uniformed and narrow-distributed nanogel exhibits high P-5m loading capacity (43.4%). Interestingly, the nanogel is stable in vitro and in vivo, showing excellent and specific MMP2-triggered payload release property. As expected, the nanogel suppresses cancer cell migration and invasion in high performance, ultimately achieving remarkable tumor metastasis inhibition in vivo.
Source: openalex_inverted_index · Quality: baseline
Research context
OpenAlex topics: Peptidase Inhibition and Analysis · Protease and Inhibitor Mechanisms · Ubiquitin and proteasome pathways
SciVX discovery tags are terminology-based. OpenAlex topics are source-provided classifications.
Affiliations
CAS Center for Excellence in Nanoscience, CAS Key Laboratory for Biomedical Effects of Nanomaterials and Nanosafety, National Center for Nanoscience and Technology (NCNST), Beijing 100190, P. R. China
University of Chinese Academy of Sciences (UCAS), Beijing 100049, P. R. China
Funding
National Natural Science Foundation of China · Chinese Academy of Sciences
References (33)
Show source-provided references
1. 10.1016/j.biomaterials.2017.11.04810.1016/j.biomaterials.2017.11.048 ↗
2. 10.1016/j.cell.2011.02.01310.1016/j.cell.2011.02.013 ↗
3. 10.1038/nrc274810.1038/nrc2748 ↗
4. 10.1126/science.120354310.1126/science.1203543 ↗
5. 10.1038/nature0720510.1038/nature07205 ↗
6. 10.1002/(SICI)1096-9896(199911)189:3<300::AID-PATH456>3.0.CO;2-C10.1002/(SICI)1096-9896(199911)189:3<300::AID-PATH456>3.0.CO;2-C ↗
7. 10.1007/s10555-006-7886-910.1007/s10555-006-7886-9 ↗
8. 10.1038/nrc74510.1038/nrc745 ↗
9. 10.1038/nrc88410.1038/nrc884 ↗
10. 10.1006/bbrc.2001.586410.1006/bbrc.2001.5864 ↗
11. 10.3390/molecules1702135710.3390/molecules17021357 ↗
12. 10.1074/jbc.M30879020010.1074/jbc.M308790200 ↗
13. 10.1002/anie.20060448810.1002/anie.200604488 ↗
14. 10.1002/anie.20025065310.1002/anie.200250653 ↗
15. 10.1038/nrd261410.1038/nrd2614 ↗
16. 10.1016/j.progpolymsci.2016.12.00410.1016/j.progpolymsci.2016.12.004 ↗
17. 10.1016/j.biomaterials.2016.09.03410.1016/j.biomaterials.2016.09.034 ↗
18. 10.1021/cr500131f10.1021/cr500131f ↗
19. 10.1021/acsami.6b0458010.1021/acsami.6b04580 ↗
20. 10.1016/j.biomaterials.2014.03.00110.1016/j.biomaterials.2014.03.001 ↗
21. 10.1038/s41467-017-01296-810.1038/s41467-017-01296-8 ↗
22. 10.1021/ar200216f10.1021/ar200216f ↗
23. 10.1002/anie.20070136810.1002/anie.200701368 ↗
24. 10.1002/anie.20100603810.1002/anie.201006038 ↗
25. 10.1002/anie.20090721010.1002/anie.200907210 ↗
26. 10.1016/j.colsurfb.2011.09.02510.1016/j.colsurfb.2011.09.025 ↗
27. 10.1002/anie.20090044110.1002/anie.200900441 ↗
28. 10.1021/acsnano.7b0337510.1021/acsnano.7b03375 ↗
29. 10.1016/j.biomaterials.2013.01.08310.1016/j.biomaterials.2013.01.083 ↗
30. 10.1021/acsami.7b0273410.1021/acsami.7b02734 ↗
31. 10.1002/adma.20140592610.1002/adma.201405926 ↗
32. 10.1021/acsnano.7b0078110.1021/acsnano.7b00781 ↗
33. 10.1016/j.matbio.2015.04.00410.1016/j.matbio.2015.04.004 ↗