MOFzyme: Intrinsic protease-like activity of Cu-MOF

Scientific Reports

Volumn 4, Issue , 2014, Pages

  Li, Bin ^a   Chen, Daomei ^a   Wang, Jiaqiang ^a   Yan, Zhiying ^a   Jiang, Liang ^a   Duan, Deliang ^a   He, Jiao ^a   Luo, Zhongrui ^a   Zhang, Jinping ^a   Yuan, Fagui ^a  

^a BEIJING UNIVERSITY OF POSTS AND TELECOMMUNICATIONS   (China)

Author keywords

[No Author keywords available]

Indexed keywords

BIS(1,3,5-BENZENETRICARBOXYLATE)TRICOPPER(II); BOVINE SERUM ALBUMIN; CASEIN; ORGANOMETALLIC COMPOUND; PROTEINASE;

CATALYSIS; CELL LINE; CHEMISTRY; HUMAN; KINETICS; METABOLISM; PROTEIN DEGRADATION;

CASEINS; CATALYSIS; CELL LINE; ENDOPEPTIDASES; HUMANS; KINETICS; ORGANOMETALLIC COMPOUNDS; PROTEOLYSIS; SERUM ALBUMIN, BOVINE;

EID: 84923345243     PISSN: None     EISSN: 20452322     Source Type: Journal    
DOI: 10.1038/srep06759     Document Type: Article

References (57)

1. Mina, K., Kim, J., Park, K. & Yoo, Y. J. Enzyme immobilization on carbon nanomaterials: Loading density investigation and zeta potential analysis. J. Mol. Catal. B-Enzym. 83, 87-93 (2012).
2. Krajewska, B. Application of chitin- and chitosan-based materials for enzyme immobilizations: a review. ZnzymeMicrob. Tech. 35, 126-139 (2004).
3. 60) derivative with superoxide dismutase mimetic properties. Free Radical Biol. Med. 37, 1191-1202 (2004).
4. Pasquato, L., Rancan, F., Scrimin, P., Mancin, F. & Frigeri, C. N-methylimidazole-functionalized gold nanoparticles as catalysts for cleavage of a carboxylic acid ester. Chem. Commun. 17, 2253-2254 (2000).
5. Comotti, M., Pina, C. D., Matarrese, R. & Rossi, M. The catalytic activity of "naked" gold particles. Angew. Chem. Int. Ed. 43, 5812-5815 (2004).
6. Chen, J., Patil, S., Seal, S. & McGinnis, J. F. Rare earth nanoparticles prevent retinal degeneration induced by intracellular peroxides. Nat. Nanotechnol. 1, 142-150 (2006).
7. Gao, L. et al. Intrinsic peroxidase-like activity of ferromagnetic nanoparticles. Nat. Nanotechnol. 2, 577-583 (2007).
8. 2 and glucose detection. Anal. Chem. 80, 2250-2254 (2008).
9. Fan, K. et al. Magnetoferritin nanoparticles for targeting and visualizing tumour tissues. Nat. Nanotechnol. 7, 459-464 (2012).
10. Manea, F., Houillon, F. B., Pasquato, L. & Scrimin, P. Nanozymes: Goldnanoparticle-based transphosphorylation catalysts. Angew. Chem. Int. Ed. 43, 6165-6169 (2004).
11. Pasquato, L., Pengo, P. & Scrimin, P. Nanozymes: Functional nanoparticle-based catalysts. Supramol. Chem. 17, 163-171 (2005).
12. 2 hydrolyzes both dipeptides and proteins. J. Am. Chem. Soc. 117, 7015-7016 (1995).
13. Kim, H. M., Jang, B., Cheon, Y. E., Suh, M. P. & Suh, J. Proteolytic activity of Co(III) complex of 1-oxa-4,7, 10-triazacyclododecane: a new catalytic center for peptide-cleavage agents. J. Biol. Inorg. Chem. 14, 151-157 (2009).
14. Wang, X., Wang, D., Liang, P. & Liang, X. Synthesis and properties of an insoluble chitosan resin modified by azamacrocycle copper(II) complex for protein hydrolysis. J. Appl. Polym. Sci. 128, 3280-3288 (2013).
15. Kassai, M., Ravi, R. G., Sarah, S. J. & Grant, K. B. Unprecedented acceleration of zirconium(IV)-assisted peptide hydrolysis at neutral pH. Inorg. Chem. 43, 6130-6132 (2004).
16. Yashiro, M., Kawakami, Y., Taya, J., Arai, S. & Fujii, Y. Zn(II) complex for selective and rapid scission of protein backbone. Chem. Commun. 12, 1544-1546 (2009).
17. Kim, M. G. et al. Soluble artificial metalloproteases with broad substrate selectivity, high reactivity, and high thermal and chemical stabilities. J. Biol. Inorg. Chem. 15, 1023-1031 (2010).
18. Yoo, S. H., Lee, B. J., Kim, H. & Suh, J. Artificial metalloprotease with active site comprising aldehyde group and Cu(II)Cyclen complex. J. Am. Chem. Soc. 127, 9593-9602 (2005).
19. Ma, S. Gas adsorption applications of porous metal-organic frameworks. Pure Appl. Chem. 81, 2235-2251 (2009).
20. Lee, J. et al. Metal-organic framework materials as catalysts. Chem. Soc. Rev. 38, 1450-1459 (2009).
21. Rowsell, J. L. C. & Yaghi, O. M. Effects of functionalization, catenation, and variation of the metal oxide and organic linking units on the low-pressure hydrogen adsorption properties of metal-organic frameworks. J. Am. Chem. Soc. 128, 1304-1315 (2006).
22. Gu, Z.-Y., Park, J., Raiff, A., Wei, Z. & Zhou, H.-C. Metal-Organic Frameworks as Biomimetic Catalysts. ChemCatChem 6, 67-75 (2014).
23. Falcaro, P. et al. A new method to position and functionalize metal-organic framework crystals. Nat. Commun. 2, 237 (2011).
24. Sun, C.-Y. et al. Efficient and tunable white-light emission of metal-organic frameworks by iridium-complex encapsulation. Nat. Commun. 4, 2717 (2013).
25. Yu, J. et al. Confinement of pyridiniumhemicyanine dye within an anionic metalorganic framework for two-photon-pumped lasing. Nat. Commun. 4, 2719 (2013).
26. Mammen, M., Choi, S.-K. & Whitesides, G. M. Polyvalent interactions in biological systems: implications for design and use of multivalent ligands and inhibitors. Angew. Chem. Int. Ed. 37, 2754-2794 (1998).
27. Feng, D. et al. Zirconium-metalloporphyrin PCN-222: mesoporous metal-organic frameworks with ultrahigh stability as biomimetic catalysts. Angew. Chem. Int. Ed. 51, 10307-10310 (2012).
28. Ai, L., Li, L., Zhang, C., Fu, J. & Jiang, J. MIL-53(Fe): a metal-organic framework with Intrinsic peroxidase-like catalytic activity for colorimetric biosensing. Chem. Eur. J. 19, 15105-15108 (2013).
29. Zhang, J. W. et al. Water-stable metal-organic frameworks with intrinsic peroxidase-like catalytic activity as a colorimetric biosensing platform. Chem. Commun. 50, 1092-1094 (2014).
30. Gu, Z.-Y., Chen, Y.-J., Jiang, J.-Q. & Yan, X.-P. Metal-organic frameworks for efficient enrichment of peptides with simultaneous exclusion of proteins from complex biological samples. Chem. Commun. 47, 4787-4789 (2011).
31. Jung, S. et al. Bio-functionalization of metal-organic frameworks by covalent protein conjugation. Chem. Commun. 47, 2904-2906 (2011).
32. Lykourinou, V. et al. Immobilization of MP-11 into a mesoporous metal-organic framework, MP-11@mesoMOF: a new platform for enzymatic catalysis. J. Am. Chem. Soc. 133, 10382-10385 (2011).
33. Chen, Y., Lykourinou, V., Hoang, T., Ming, L.-J. & Ma, S. Size-selective biocatalysis of myoglobin immobilized into a mesoporous metal-organic framework with hierarchical pore sizes. Inorg. Chem. 51, 9156-9158 (2012).
34. Larsen, R. W. et al. Mimicking heme enzymes in the solid state: metal-organic materials with selectively encapsulated heme. J. Am. Chem. Soc. 133, 10356-10359 (2011).
35. Qin, F.-X. et al. Hemin@metal-organic framework with peroxidaselike activity and its application to glucose detection. Catal. Sci. Technol. 3, 2761-2768 (2013).
36. Shih, Y.-H. et al. Novel trypsin-FITC@MOF bioreactor efficiently catalyzes protein digestion. ChemPlusChem. 77, 982-986 (2012)
37. Liu, W.-L. et al. Trypsin-immobilized metal-organic framework as a biocatalyst in proteomics analysis. J. Mater. Chem. B 1, 928-932 (2013).
38. Jang, B.-B., Lee, K.-P., Min, D.-H. & Suh, J. Immobile artificial metalloproteinase containing both catalytic and binding groups. J. Am. Chem. Soc. 120, 12008-12016 (1998).
39. 2). Adv. Mater. 25, 1052-1057 (2013).
40. 2 and UiO-66. Micropor. Mesopor. Mat. 179, 48-53 (2013).
41. Kim, J., Cho, H.-Y. & Ahn, W.-S. Synthesis and adsorption/catalytic properties of the metalorganic framework CuBTC. Catal. Surv. Asia 16, 106-119 (2012).
42. 3n. Science 283, 1148-1150 (1998).
43. 2. Micropor. Mesocpor. Mat. 73, 81-88 (2004).
44. Petit, C., Burress, J. & Bandosz, T. J. The synthesis and characterization of copperbased metal-organic framework/graphite oxide composites. Carbon 49, 563-572 (2011).
45. Vairam, S. & Govindarajan, S. New hydrazinium salts of benzene tricarboxylic and tetracarboxylicacid-spreparation and their thermal studies. Thermochimica Acta 414, 263-270 (2004).
46. Kim, H. et al. Effective artificial proteases synthesized by covering silica gel with aldehyde and various other organic groups. Bioorg. Med. Chem. Lett. 12, 3247-3250 (2002).
47. Yoo, C. E., Chae, P. S., Kim, J. E., Jeong, E. J. & Suh, J. Degradation of myoglobin by polymeric artificial metalloproteases containing catalytic modules with various catalytic group densities: site selectivity in peptide bond cleavage. J. Am. Chem. Soc. 125, 14580-14589 (2003).
48. Suh, J. & Oh, S. Remarkable proteolytic activity of imidazoles attached to crosslinked polystyrene. J. Org. Chem. 65, 7534-7540 (2000).
49. Ram, J. S. & Maurer, P. H. Modified bovine serum albumin. III. hydrolysis studies with trypsin, chymotrypsin and pepsin. Arch. Biochem. Biophys. 70, 185-204 (1957).
50. Jang, S. W. & Suh, J. Proteolytic activity of Cu(II) complex of 1-Oxa-4,7,10-triazacyclododecane. Org. Lett. 10, 481-484 (2008).
51. Swain, S. K. & Sarkar, D. Study of BSA protein adsorption/release on hydroxyapatite nanoparticles. Appl. Surf. Sci. 286, 99-103 (2013).
52. Zeng, G. et al. Effect of monorhamnolipid on the degradation of n-hexadecane by Candida tropicalis and the association with cell surface properties. Appl. Microbiol. Biotechnol. 90, 1155-1161 (2011).
53. 4] Clusters. Inorg. Chem. 52, 2880-2890 (2013).
54. Dalgleish, D. G. On the structural models of bovine casein micelles-review and possible improvements. Soft Matter 7, 2265-2272 (2011).
55. Jollès, P. Progress in the chemistry of casein. Angew. Chem. Int. Edit. 6, 558-566 (1966).
56. Olsen, J. V., Ong, S. E. & Mann, M. Trypsin cleaves exclusively C-terminal to arginine and lysine residues. Mol. Cell Proteomics 3, 608-614 (2004).
57. Wiester, M. J., Ulmann, P. A. & Mirkin, C. A. Enzyme mimics based upon supramolecular coordination chemistry. Angew. Chem. Int. Ed. 50, 114-137 (2011).