Preserving the adhesion of catechol-conjugated hydrogels by thiourea–quinone coupling
Source abstract
Abstract
Mussel adhesion has inspired the development of catechol-based adhesive polymers. However, conventional strategies require basic pH conditions and lead to the loss of adhesion. To solve the problem, we report the first attempt to use thiourea-functionalized polymers for preserving hydrogel adhesion. We believe that this simple thiourea-quinone coupling chemistry is instrumental to synthetic adhesive materials.
Source: openalex_inverted_index · Quality: candidate unverified · Source record ↗
Research context
OpenAlex topics: Polymer Surface Interaction Studies · Molecular Junctions and Nanostructures · Nanofabrication and Lithography Techniques
SciVX discovery tags are terminology-based. OpenAlex topics are source-provided classifications.
Affiliations
Division of Biomedical Engineering
The Chinese University of Hong Kong
The People's Republic of China
Department of Mechanical and Automation Engineering
Funding
Research Grants Council, University Grants Committee, Hong Kong
References (34)
Show source-provided references
1. Maier · Science · 2015 · 349 · 62810.1126/science.aab0556 ↗
2. Yu · Nat. Chem. Biol. · 2011 · 7 · 58810.1038/nchembio.630 ↗
3. Anderson · Adv. Funct. Mater. · 2010 · 20 · 419610.1002/adfm.201000932 ↗
4. Kan · PLoS One · 2014 · 9 · e10886910.1371/journal.pone.0108869 ↗
5. Wei · J. Am. Chem. Soc. · 2012 · 135 · 37710.1021/ja309590f ↗
6. Yu · Adv. Mater. · 2011 · 23 · 236210.1002/adma.201003580 ↗
7. Hwang · J. Mater. Chem. · 2012 · 22 · 1553010.1039/c2jm32439c ↗
8. Yu · Biomacromolecules · 2013 · 14 · 107210.1021/bm301908y ↗
9. Lee · Biomacromolecules · 2002 · 3 · 103810.1021/bm025546n ↗
10. Cencer · Biomacromolecules · 2014 · 15 · 286110.1021/bm500701u ↗
11. Kim · Biomacromolecules · 2014 · 15 · 157910.1021/bm4017308 ↗
12. Hong · Adv. Funct. Mater. · 2013 · 23 · 177410.1002/adfm.201202365 ↗
13. Danner · Biochemistry · 2012 · 51 · 651110.1021/bi3002538 ↗
14. Lee · Proc. Natl. Acad. Sci. U. S. A. · 2006 · 103 · 1299910.1073/pnas.0605552103 ↗
15. Nicklisch · Biofouling · 2012 · 28 · 86510.1080/08927014.2012.719023 ↗
16. Zhao · J. Biol. Chem. · 2006 · 281 · 2615010.1074/jbc.M604357200 ↗
17. Martinez Rodriguez · Biofouling · 2015 · 31 · 22110.1080/08927014.2015.1026337 ↗
18. Nicklisch · Biotechnol. Prog. · 2013 · 29 · 158710.1002/btpr.1810 ↗
19. Harris · IUBMB Life · 2002 · 53 · 8510.1080/15216540211468 ↗
20. Schiessl · Z. Anorg. Allg. Chem. · 2005 · 631 · 281210.1002/zaac.200500157 ↗
21. Abdel-Mohsen · J. Org. Chem. · 2013 · 78 · 798610.1021/jo401193e ↗
22. Hong · Beilstein J. Nanotechnol. · 2014 · 5 · 88710.3762/bjnano.5.101 ↗
23. Park · Chem. Mater. · 2015 · 27 · 10510.1021/cm503425d ↗
24. Wang · ACS Catal. · 2014 · 4 · 96210.1021/cs401096c ↗
25. Ji · J. Am. Chem. Soc. · 2012 · 134 · 600610.1021/ja300724x ↗
26. Medintz · Nat. Mater. · 2010 · 9 · 67610.1038/nmat2811 ↗
27. Liu · ACS Appl. Mater. Interfaces · 2014 · 6 · 1698210.1021/am504566v ↗
28. Xu · ACS Macro Lett. · 2012 · 1 · 45710.1021/mz200217d ↗
29. Andersen · Biochim. Biophys. Acta, Protein Struct. Mol. Enzymol. · 1992 · 1118 · 13410.1016/0167-4838(92)90140-9 ↗
30. Land · Org. Biomol. Chem. · 2009 · 7 · 94410.1039/b819367c ↗
31. Borovansky · Pigm. Cell Res. · 2006 · 19 · 17010.1111/j.1600-0749.2006.00295.x ↗
32. Matos-Perez · J. Am. Chem. Soc. · 2012 · 134 · 949810.1021/ja303369p ↗
33. Bre · Biomater. Sci. · 2013 · 1 · 23910.1039/C2BM00121G ↗
34. Kim · Biomater. Sci. · 2013 · 1 · 78310.1039/c3bm00004d ↗