Highly Sensitive Assay for Acetylcholinesterase Activity and Inhibition Based on a Specifically Reactive Photonic Nanostructure
Source abstract
Abstract
Assays for acetylcholinesterase (AChE) with high sensitivity and high selectivity as well as facile manipulation have been urgently required in various fields. In this work, a reaction-based photonic strategy was developed for the efficient assay of AChE activity and inhibition based on the synergetic combination of the specific thiol-maleimide addition reaction with photonic porous structure. It was found that various applications including detection of AChE activity, measurement of the related enzymatic kinetics, and screening of inhibitors could be efficiently implemented using such strategy. Remarkably, the unique photonic nanostructure endows the constructed sensing platform with high sensitivity with a limit of detection (LOD) of 5 mU/mL for AChE activity, high selectivity, and self-reporting signaling. Moreover, the label-free solid film-based sensing approach described here has advantages of facile manipulation and bare-eye readout, compared with conventional liquid-phase methods, exhibiting promising potential in practical application for the AChE assay.
Source: openalex_inverted_index · Quality: baseline
Research context
OpenAlex topics: Cholinesterase and Neurodegenerative Diseases · Electrochemical sensors and biosensors · Advanced Nanomaterials in Catalysis
SciVX discovery tags are terminology-based. OpenAlex topics are source-provided classifications.
Affiliations
Key Lab of Organic Optoelectronics and Molecular Engineering, Department of Chemistry, Tsinghua University, Beijing 100084, China
Funding
Ministry of Science and Technology of the People's Republic of China · Deutsche Forschungsgemeinschaft · National Natural Science Foundation of China
References (53)
Show source-provided references
1. Quinn D. M. · Chem. Rev. · 1987 · 87 · 95510.1021/cr00081a005 ↗
2. Whittaker V. P. · Trends Pharmacol. Sci. · 1990 · 11 · 810.1016/0165-6147(90)90034-6 ↗
3. Ballard C. G. · Eur. Neurol. · 2002 · 47 · 6410.1159/000047952 ↗
4. Ashani Y. · Biochem. Biophys. Res. Commun. · 1992 · 184 · 71910.1016/0006-291X(92)90649-6 ↗
5. Tougu V. · Curr. Med. Chem.: Cent. Nerv. Syst. Agents · 2001 · 1 · 155
6. Bartolini M. · Biochem. Pharmacol. · 2003 · 65 · 40710.1016/S0006-2952(02)01514-9 ↗
7. Pope C. N. · J. Toxicol. Environ. Health, B · 1999 · 2 · 16110.1080/109374099281205 ↗
8. Fukuto T. R. · Environ. Health Perspect. · 1990 · 87 · 24510.1289/ehp.9087245 ↗
9. Miao Y. · Chem. Rev. · 2010 · 110 · 521610.1021/cr900214c ↗
10. Ellman G. L. · Arch. Biochem. Biophys. · 1959 · 82 · 7010.1016/0003-9861(59)90090-6 ↗
11. Birman S. · Biochem. J. · 1985 · 225 · 82510.1042/bj2250825 ↗
12. Rhee I. K. · Phytochem. Anal. · 2003 · 14 · 12710.1002/pca.675 ↗
13. Maeda H. · Angew. Chem., Int. Ed. · 2005 · 44 · 292210.1002/anie.200500114 ↗
14. Pavlov V. · Nano Lett. · 2005 · 5 · 64910.1021/nl050054c ↗
15. Liu D. · Adv. Healthcare Mater. · 2012 · 1 · 9010.1002/adhm.201100002 ↗
16. Peng L. · Org. Lett. · 2009 · 11 · 401410.1021/ol9016723 ↗
17. Feng F. · Angew. Chem., Int. Ed. · 2007 · 46 · 788210.1002/anie.200701724 ↗
18. Li Y. · ACS Appl. Mater. Interfaces · 2011 · 3 · 130610.1021/am200101n ↗
19. Pardo-Yissar V. · J. Am. Chem. Soc. · 2003 · 125 · 62210.1021/ja028922k ↗
20. Lu D. · Adv. Funct. Mater. · 2011 · 21 · 437110.1002/adfm.201100616 ↗
21. Lévy R. · J. Am. Chem. Soc. · 2004 · 126 · 1007610.1021/ja0487269 ↗
22. Guo L. · J. Am. Chem. Soc. · 2013 · 135 · 1233810.1021/ja405371g ↗
23. Storhoff J. J. · J. Am. Chem. Soc. · 2000 · 122 · 464010.1021/ja993825l ↗
24. Li X. · Small · 2012 · 8 · 61210.1002/smll.201101934 ↗
25. Yablonovitch E. · Phys. Rev. Lett. · 1987 · 58 · 205910.1103/PhysRevLett.58.2059 ↗
26. John S. · Phys. Rev. Lett. · 1987 · 58 · 248610.1103/PhysRevLett.58.2486 ↗
27. Aguirre C. I. · Adv. Funct. Mater. · 2010 · 20 · 256510.1002/adfm.201000143 ↗
28. Zhao Y. · Chem. Soc. Rev. · 2012 · 41 · 329710.1039/c2cs15267c ↗
29. Ge J. · Angew. Chem., Int. Ed. · 2011 · 50 · 149210.1002/anie.200907091 ↗
30. Scheid D. · J. Mater. Chem. C · 2014 · 2 · 258310.1039/c3tc32525c ↗
31. González-Urbina L. · Chem. Rev. · 2012 · 112 · 226810.1021/cr200063f ↗
32. Schäfer C. G. · Chem. Mater. · 2013 · 25 · 230910.1021/cm400911j ↗
33. Li H. · Adv. Funct. Mater. · 2008 · 18 · 325810.1002/adfm.200800507 ↗
34. Tian E. · J. Mater. Chem. · 2008 · 18 · 111610.1039/b717368g ↗
35. Liu C. · Macromol. Rapid Commun. · 2012 · 33 · 38010.1002/marc.201100575 ↗
36. Walker J. P. · Anal. Chem. · 2005 · 77 · 159610.1021/ac048562e ↗
37. Tan E. V. · Anal. Chem. · 2009 · 81 · 757910.1021/ac9008989 ↗
38. Marrian D. H. · J. Chem. Soc. (Resumed) · 1949 · 151510.1039/jr9490001515 ↗
39. Ghosh S. S. · Bioconjugate Chem. · 1990 · 1 · 7110.1021/bc00001a009 ↗
40. Pounder R. J. · Chem. Commun. · 2008 · 515810.1039/b809167f ↗
41. Flory P. J. · J. Chem. Phys. · 1950 · 18 · 10810.1063/1.1747424 ↗
42. Yang H. · J. Mater. Chem. C · 2013 · 1 · 612010.1039/c3tc30127c ↗
43. Zhao Y. · Adv. Funct. Mater. · 2010 · 20 · 297010.1002/adfm.201000098 ↗
44. Takeoka Y. · Langmuir · 2002 · 18 · 597710.1021/la020133t ↗
45. Mantovani G. · J. Am. Chem. Soc. · 2005 · 127 · 296610.1021/ja0430999 ↗
46. Aguiar E. C. · J. Mol. Struct. · 2011 · 993 · 43110.1016/j.molstruc.2010.10.042 ↗
47. Haddad G. L. · Angew. Chem., Int. Ed. · 2012 · 51 · 1112610.1002/anie.201203640 ↗
48. Larsson R. · Angew. Chem., Int. Ed. · 2004 · 43 · 371610.1002/anie.200454165 ↗
49. Lineweaver H. · J. Am. Chem. Soc. · 1934 · 56 · 65810.1021/ja01318a036 ↗
50. Wang M. · Anal. Chem. · 2009 · 81 · 444410.1021/ac9002722 ↗
51. Nakayama D. · Angew. Chem., Int. Ed. · 2003 · 42 · 419710.1002/anie.200351746 ↗
52. Wang X. · Food Chem. · 2013 · 141 · 394710.1016/j.foodchem.2013.06.024 ↗
53. Meng L. · Anal. Chim. Acta · 2013 · 771 · 8610.1016/j.aca.2013.01.055 ↗