Journal Home > Volume 9 , Issue 8
Nano Research 2016, 9(8): 2411-2423 https://doi.org/10.1007/s12274-016-1127-5
Research Article | Issue | Published: 01 June 2016

Platinum-coordinated graphitic carbon nitride nanosheet used for targeted inhibition of amyloid β-peptide aggregation

Show Author's Information Meng Li1,2,  Yijia Guan1,2,  Zhaowei Chen1,2,  Nan Gao1,  Jinsong Ren1,  Kai Dong1,2,  Xiaogang Qu1( )
Laboratory of Chemical Biology and State Key Laboratory of Rare Earth Resource UtilizationChangchun Institute of Applied ChemistryChinese Academy of SciencesChangchun130022China
University of Chinese Academy of SciencesBeijing100039China
Keywords:
platinum, amyloid disease, graphitic carbon nitride nanosheet, photooxygenation, amyloid β-peptide (Aβ) inhibitors
Cite this article:
Li M, Guan Y, Chen Z, et al. Platinum-coordinated graphitic carbon nitride nanosheet used for targeted inhibition of amyloid β-peptide aggregation. Nano Research, 2016, 9(8): 2411-2423. https://doi.org/10.1007/s12274-016-1127-5
Download citation
EndNote(RIS)
BibTeX

678

Views

14

Downloads

Citations

34

Crossref

N/A

WoS

35

Scopus

4

CSCD

Abstract Full text Electronic supplementary material About this article

Amyloid β-peptide (Aβ) aggregation is a critical step in the pathogenesis of Alzheimer's disease (AD). Inhibition of Aβ production, dissolution of existing aggregates and clearance of Aβ represent valid therapeutic strategies against AD. Herein, a novel platinum(Ⅱ)-coordinated graphitic carbon nitride (g-C3N4) nanosheet (g-C3N4@Pt) has been designed to covalently bind to Aβ and modulate the peptide's aggregation and toxicity. Furthermore, g-C3N4@Pt nanosheets possess high photocatalytic activity and can oxygenate Aβ upon visible light irradiation, remarkably attenuating both the aggregation potency and neurotoxicity of Aβ. Due to its ability to cross the blood-brain barrier (BBB) and its good biocompatibility, g-C3N4@Pt nanosheet is a promising inhibitor of Aβ aggregation. This study may serve as a model for the engineering of novel multifunctional nanomaterials used for the treatment of AD.


menu
Abstract
Full text
Outline
Electronic supplementary material
About this article

Platinum-coordinated graphitic carbon nitride nanosheet used for targeted inhibition of amyloid β-peptide aggregation

Show Author's information Meng Li1,2, Yijia Guan1,2, Zhaowei Chen1,2, Nan Gao1, Jinsong Ren1, Kai Dong1,2, Xiaogang Qu1( )
Laboratory of Chemical Biology and State Key Laboratory of Rare Earth Resource UtilizationChangchun Institute of Applied ChemistryChinese Academy of SciencesChangchun130022China
University of Chinese Academy of SciencesBeijing100039China

Abstract

Amyloid β-peptide (Aβ) aggregation is a critical step in the pathogenesis of Alzheimer's disease (AD). Inhibition of Aβ production, dissolution of existing aggregates and clearance of Aβ represent valid therapeutic strategies against AD. Herein, a novel platinum(Ⅱ)-coordinated graphitic carbon nitride (g-C3N4) nanosheet (g-C3N4@Pt) has been designed to covalently bind to Aβ and modulate the peptide's aggregation and toxicity. Furthermore, g-C3N4@Pt nanosheets possess high photocatalytic activity and can oxygenate Aβ upon visible light irradiation, remarkably attenuating both the aggregation potency and neurotoxicity of Aβ. Due to its ability to cross the blood-brain barrier (BBB) and its good biocompatibility, g-C3N4@Pt nanosheet is a promising inhibitor of Aβ aggregation. This study may serve as a model for the engineering of novel multifunctional nanomaterials used for the treatment of AD.

Keywords: platinum, amyloid disease, graphitic carbon nitride nanosheet, photooxygenation, amyloid β-peptide (Aβ) inhibitors

References(66)

1

Hardy, J.; Selkoe, D. J. The amyloid hypothesis of Alzheimer's disease: Progress and problems on the road to therapeutics. Science 2002, 297, 353-356.
DOI Google Scholar
2

Hamley, I. W. The amyloid beta peptide: A chemist's perspective. Role in Alzheimer's and fibrillization. Chem. Rev. 2012, 112, 5147-5192.
DOI Google Scholar
3

Jakob-Roetne, R.; Jacobsen, H. Alzheimer's disease: From pathology to therapeutic approaches. Angew. Chem., Int. Ed. 2009, 48, 3030-3059.
DOI Google Scholar
4

Gaggelli, E.; Kozlowski, H.; Valensin, D.; Valensin, G. Copper homeostasis and neurodegenerative disorders (Alzheimer's, prion, and Parkinson's diseases and amyotrophic lateral sclerosis). Chem. Rev. 2006, 106, 1995-2044.
DOI Google Scholar
5

Takeda, S.; Sato, N.; Uchio-Yamada, K.; Sawada, K.; Kunieda, T.; Takeuchi, D.; Kurinami, H.; Shinohara, M.; Rakugi, H.; Morishita, R. Diabetes-accelerated memory dysfunction via cerebrovascular inflammation and Aβ deposition in an Alzheimer mouse model with diabetes. Proc. Natl. Acad. Sci. USA 2010, 107, 7036-7041.
DOI Google Scholar
6

Jin, M.; Shepardson, N.; Yang, T.; Chen, G.; Walsh, D.; Selkoe, D. J. Soluble amyloid β-protein dimers isolated from Alzheimer cortex directly induce Tau hyperphosphorylation and neuritic degeneration. Proc. Natl. Acad. Sci. USA 2011, 108, 5819-5824.
DOI Google Scholar
7

De Felice, F. G.; Vieira, M. N. N.; Bomfim, T. R.; Decker, H.; Velasco, P. T.; Lambert, M. P.; Viola, K. L.; Zhao, W. Q.; Ferreira, S. T.; Klein, W. L. Protection of synapses against Alzheimer's-linked toxins: Insulin signaling prevents the pathogenic binding of Abeta oligomers. Proc. Natl. Acad. Sci. USA 2009, 106, 1971-1976.
DOI Google Scholar
8

Ono, K.; Condron, M. M.; Teplow, D. B. Structure- neurotoxicity relationships of amyloid β-protein oligomers. Proc. Natl. Acad. Sci. USA 2009, 106, 14745-14750.
DOI Google Scholar
9

Takahashi, T.; Mihara, H. Peptide and protein mimetics inhibiting amyloid β-peptide aggregation. Acc. Chem. Res. 2008, 41, 1309-1318.
DOI Google Scholar
10

Frydman-Marom, A.; Rechter, M.; Shefler, I.; Bram, Y.; Shalev, D. E.; Gazit, E. Cognitive-performance recovery of Alzheimer's disease model mice by modulation of early soluble amyloidal assemblies. Angew. Chem., Int. Ed. 2009, 48, 1981-1986.
DOI Google Scholar
11

Tjernberg, L. O.; Näslund, J.; Lindqvist, F.; Johansson, J.; Karlström, A. R.; Thyberg, J.; Terenius, L.; Nordstedt, C. Arrest of β-amyloid fibril formation by a pentapeptide ligand. J. Biol. Chem. 1996, 271, 8545-8548.
DOI Google Scholar
12

Ehrnhoefer, D. E.; Bieschke, J.; Boeddrich, A.; Herbst, M.; Masino, L.; Lurz, R.; Engemann, S.; Pastore, A.; Wanker, E. E. EGCG redirects amyloidogenic polypeptides into unstructured, off-pathway oligomers. Nat. Struct. Mol. Biol. 2008, 15, 558-566.
DOI Google Scholar
13

Matlack, K. E. S.; Tardiff, D. F.; Narayan, P.; Hamamichi, S.; Caldwell, K. A.; Caldwell, G. A.; Lindquist, S. Clioquinol promotes the degradation of metal-dependent amyloid-β (Aβ) oligomers to restore endocytosis and ameliorate Aβ toxicity. Proc. Natl. Acad. Sci. USA 2014, 111, 4013-4018.
DOI Google Scholar
14

Barnham, K. J.; Kenche, V. B.; Ciccotosto, G. D.; Smith, D. P.; Tew, D. J.; Liu, X.; Perez, K.; Cranston, G. A.; Johanssen, T. J.; Volitakis, I. et al. Platinum-based inhibitors of amyloid-β as therapeutic agents for Alzheimer's disease. Proc. Natl. Acad. Sci. USA 2008, 105, 6813-6818.
DOI Google Scholar
15

Hureau, C.; Faller, P. Platinoid complexes to target monomeric disordered peptides: A forthcoming solution against amyloid diseases? Dalton Trans. 2014, 43, 4233-4237.
DOI Google Scholar
16

Scott, L. E.; Orvig, C. Medicinal inorganic chemistry approaches to passivation and removal of aberrant metal ions in disease. Chem. Rev. 2009, 109, 4885-4910.
DOI Google Scholar
17

Cassagnes, L. -E.; Hervé, V.; Nepveu, F.; Hureau, C.; Faller, P.; Collin, F. The catalytically active copper-amyloid-beta state: Coordination site responsible for reactive oxygen species production. Angew. Chem., Int. Ed. 2013, 52, 11110-11113.
DOI Google Scholar
18

Lim, S.; Paterson, B. M.; Fodero-Tavoletti, M. T.; O'Keefe, G. J.; Cappai, R.; Barnham, K. J.; Villemagne, V. L.; Donnelly, P. S. A copper radiopharmaceutical for diagnostic imaging of Alzheimer's disease: A bis(thiosemicarbazonato)copper(Ⅱ) complex that binds to amyloid-β plaques. Chem. Commun. 2010, 46, 5437-5439.
DOI Google Scholar
19

Ma, G. L.; Huang, F.; Pu, X. W.; Jia, L. Y.; Jiang, T.; Li, L. Z.; Liu, Y. Z. Identification of[PtCl2(phen)] binding modes in amyloid-β peptide and the mechanism of aggregation inhibition. Chem. -Eur. J. 2011, 17, 11657-11666.
DOI Google Scholar
20

Kenche, V. B.; Hung, L. W.; Perez, K.; Volitakes, I.; Ciccotosto, G.; Kwok, J.; Critch, N.; Sherratt, N.; Cortes, M.; Lal, V. et al. Development of a platinum complex as an anti-amyloid agent for the therapy of Alzheimer's disease. Angew. Chem., Int. Ed. 2013, 52, 3374-3378.
DOI Google Scholar
21

Man, B. Y. -W.; Chan, H. -M.; Leung, C. -H.; Chan, D. S. -H.; Bai, L. -P.; Jiang, Z. -H.; Li, H. -W.; Ma, D. -L. Group 9 metal-based inhibitors of β-amyloid (1-40) fibrillation as potential therapeutic agents for Alzheimer's disease. Chem. Sci. 2011, 2, 917-921.
DOI Google Scholar
22

Cabaleiro-Lago, C.; Quinlan-Pluck, F.; Lynch, I.; Lindman, S.; Minogue, A. M.; Thulin, E.; Walsh, D. M.; Dawson, K. A.; Linse, S. Inhibition of amyloid β protein fibrillation by polymeric nanoparticles. J. Am. Chem. Soc. 2008, 130, 15437-15443.
DOI Google Scholar
23

Yoo, S. I.; Yang, M.; Brender, J. R.; Subramanian, V.; Sun, K.; Joo, N. E.; Jeong, S. -H.; Ramamoorthy, A.; Kotov, N. A. Inhibition of amyloid peptide fibrillation by inorganic nanoparticles: Functional similarities with proteins. Angew. Chem., Int. Ed. 2011, 50, 5110-5115.
DOI Google Scholar
24

Mahmoudi, M.; Akhavan, O.; Ghavami, M.; Rezaeeef, F.; Ghiasi, S. M. A. Graphene oxide strongly inhibits amyloid beta fibrillation. Nanoscale 2012, 4, 7322-7325.
DOI Google Scholar
25

Zheng, Y.; Jiao, Y.; Chen, J.; Liu, J.; Liang, J.; Du, A. J.; Zhang, W. M.; Zhu, Z. H.; Smith, S. C.; Jaroniec, M. et al. Nanoporous graphitic-C3N4@carbon metal-free electrocatalysts for highly efficient oxygen reduction. J. Am. Chem. Soc. 2011, 133, 20116-20119.
DOI Google Scholar
26

Yan, S. C.; Li, Z. S.; Zou, Z. G. Photodegradation performance of g-C3N4 fabricated by directly heating melamine. Langmuir 2009, 25, 10397-10401.
DOI Google Scholar
27

Komatsu, T. Attempted chemical synthesis of graphite-like carbon nitride. J. Mater. Chem. 2001, 11, 799-801.
DOI Google Scholar
28

Zheng, Y.; Lin, L. H.; Wang, B.; Wang, X. C. Graphitic carbon nitride polymers toward sustainable photoredox catalysis. Angew. Chem., Int. Ed. 2015, 54, 12868-12884.
DOI Google Scholar
29

Zhang, J. S.; Chen, Y.; Wang, X. C. Two-dimensional covalent carbon nitride nanosheets: Synthesis, functionalization, and applications. Energy Environ. Sci. 2015, 8, 3092-3108.
DOI Google Scholar
30

Hou, Y.; Wen, Z. H.; Cui, S. M.; Guo, X. R.; Chen, J. H. Constructing 2D porous graphitic C3N4 nanosheets/ nitrogen-doped graphene/layered MoS2 ternary nanojunction with enhanced photoelectrochemical activity. Adv. Mater. 2013, 25, 6291-6297.
DOI Google Scholar
31

Fang, Y.; Lv, Y. Y.; Che, R. C.; Wu, H. Y.; Zhang, X. H.; Gu, D.; Zheng, G. F.; Zhao, D. Y. Two-dimensional mesoporous carbon nanosheets and their derived graphene nanosheets: Synthesis and efficient lithium ion storage. J. Am. Chem. Soc. 2013, 135, 1524-1530.
DOI Google Scholar
32

Tian, J. Q.; Liu, Q.; Ge, C. J.; Xing, Z. C.; Asiri, A. M.; Al-Youbi, A. O.; Sun, X. P. Ultrathin graphitic carbon nitride nanosheets: A low-cost, green, and highly efficient electrocatalyst toward the reduction of hydrogen peroxide and its glucose biosensing application. Nanoscale 2013, 5, 8921-8924.
DOI Google Scholar
33

Wang, Q. B.; Wang, W.; Lei, J. P.; Xu, N.; Gao, F. L.; Ju, H. X. Fluorescence quenching of carbon nitride nanosheet through its interaction with DNA for versatile fluorescence sensing. Anal. Chem. 2013, 85, 12182-12188.
DOI Google Scholar
34

Zhang, X. D.; Xie, X.; Wang, H.; Zhang, J. J.; Pan, B. C.; Xie, Y. Enhanced photoresponsive ultrathin graphitic-phase C3N4 nanosheets for bioimaging. J. Am. Chem. Soc. 2013, 135, 18-21.
DOI Google Scholar
35

Lee, E. Z.; Jun, Y. S.; Hong, W. H.; Thomas, A.; Jin, M. M. Cubic mesoporous graphitic carbon(IV) nitride: An all-in-one chemosensor for selective optical sensing of metal ions. Angew. Chem., Int. Ed. 2010, 49, 9706-9710.
DOI Google Scholar
36

Tang, Y. R.; Song, H. J.; Su, Y. Y.; Lv, Y. Turn-on persistent luminescence probe based on graphitic carbon nitride for imaging detection of biothiols in biological fluids. Anal. Chem. 2013, 85, 11876-11884.
DOI Google Scholar
37

Li, M.; Zhao, C. Q.; Yang, X. J.; Ren, J. S.; Xu, C.; Qu, X. G. In situ monitoring Alzheimer's disease β-amyloid aggregation and screening of Aβ inhibitors using a perylene probe. Small 2013, 9, 52-55.
DOI Google Scholar
38

Klement, K.; Wieligmann, K.; Meinhardt, J.; Hortschansky, P.; Richter, W.; Fändrich, M. Effect of different salt ions on the propensity of aggregation and on the structure of Alzheimer's abeta(1-40) amyloid fibrils. J. Mol. Biol. 2007, 373, 1321-1333.
DOI Google Scholar
39

Wang, X. C.; Maeda, K.; Thomas, A.; Takanabe, K.; Xin, G.; Carlsson, J. M.; Domen, K.; Antonietti, M. A metal-free polymeric photocatalyst for hydrogen production from water under visible light. Nat. Mater. 2009, 8, 76-80.
DOI Google Scholar
40

Su, F. Z.; Mathew, S. C.; Lipner, G.; Fu, X. Z.; Antonietti, M.; Blechert, S.; Wang, X. C. mpg-C3N4-catalyzed selective oxidation of alcohols using O2 and visible light. J. Am. Chem. Soc. 2010, 132, 16299-16301.
DOI Google Scholar
41

Dong, F.; Wu, L. W.; Sun, Y. J.; Fu, M.; Wu, Z. B.; Lee, S. C. Efficient synthesis of polymeric g-C3N4 layered materials as novel efficient visible light driven photocatalysts. J. Mater. Chem. 2011, 21, 15171-15174.
DOI Google Scholar
42

Shalom, M.; Molinari, V.; Esposito, D.; Clavel, G.; Ressnig, D.; Giordano, C.; Antonietti, M. Sponge-like nickel and nickel nitride structures for catalytic applications. Adv. Mater. 2014, 26, 1272-1276.
DOI Google Scholar
43

Geng, J.; Li, M.; Ren, J. S.; Wang, E. B.; Qu, X. G. Polyoxometalates as inhibitors of the aggregation of amyloid β peptides associated with Alzheimer's disease. Angew. Chem., Int. Ed. 2011, 50, 4184-4188.
DOI Google Scholar
44

Yu, H. J.; Li, M.; Liu, G. P.; Geng, J.; Wang, J. Z.; Ren, J. S.; Zhao, C. Q.; Qu, X. G. Metallosupramolecular complex targeting an α/β discordant stretch of amyloid β peptide. Chem. Sci. 2012, 3, 3145-3153.
DOI Google Scholar
45

Schlamadinger, D. E.; Kats, D. I.; Kim, J. E. Quenching of tryptophan fluorescence in unfolded cytochrome c: A biophysics experiment for physical chemistry students. J. Chem. Educ. 2010, 87, 961-964.
DOI Google Scholar
46

Puchalski, M. M.; Morra, M. J.; von Wandruszka, R. Assessment of inner filter effect corrections in fluorimetry. Fresenius J. Anal. Chem. 1991, 340, 341-344.
DOI Google Scholar
47

Cheng, N. Y.; Tian, J. Q.; Liu, Q.; Ge, C. J.; Qusti, A. H.; Asiri, A. M.; Al-Youbi, A. O.; Sun, X. P. Au-nanoparticle- loaded graphitic carbon nitride nanosheets: Green photocatalytic synthesis and application toward the degradation of organic pollutants. ACS Appl. Mater. Interfaces 2013, 5, 6815-6819.
DOI Google Scholar
48

Pei, W. B.; Wu, J. S.; Liu, J. L.; Ren, X. M.; Shen, L. J. Ion-pair complexes with strong near infrared absorbance: Syntheses, crystal structures and spectroscopic properties. Spectrochim. Acta A Mol. Biomol. Spectrosc. 2010, 75, 191-197.
DOI Google Scholar
49

Tian, J. Q.; Liu, Q.; Asiri, A. M.; Al-Youbi, A. O.; Sun, X. P. Ultrathin graphitic carbon nitride nanosheet: A highly efficient fluorosensor for rapid, ultrasensitive detection of Cu2+. Anal. Chem. 2013, 85, 5595-5599.
DOI Google Scholar
50

Li, M.; Xu, C.; Wu, L.; Ren, J. S.; Wang, E. B.; Qu, X. G. Self-assembled peptide-polyoxometalate hybrid nanospheres: Two in one enhances targeted inhibition of amyloid β-peptide aggregation associated with Alzheimer's disease. Small 2013, 9, 3455-3461.
DOI Google Scholar
51

Mishra, R.; Bulic, B.; Sellin, D.; Jha, S.; Waldmann, H.; Winter, R. Small-molecule inhibitors of islet amyloid polypeptide fibril formation. Angew. Chem., Int. Ed. 2008, 47, 4679-4682.
DOI Google Scholar
52

Li, M.; Yang, X. J.; Ren, J. S.; Qu, K. G.; Qu, X. G. Using graphene oxide high near-infrared absorbance for photothermal treatment of Alzheimer's disease. Adv. Mater. 2012, 24, 1722-1728.
DOI Google Scholar
53

Petkova, A. T.; Leapman, R. D.; Guo, Z. H.; Yau, W. -M.; Mattson, M. P.; Tycko, R. Self-propagating, molecular-level polymorphism in Alzheimer's beta-amyloid fibrils. Science 2005, 307, 262-265.
DOI Google Scholar
54

Balducci, C.; Beeg, M.; Stravalaci, M.; Bastone, A.; Sclip, A.; Biasini, E.; Tapella, L.; Colombo, L.; Manzoni, C.; Borsello, T. et al. Synthetic amyloid-β oligomers impair long-term memory independently of cellular prion protein. Proc. Natl. Acad. Sci. USA 2010, 107, 2295-2300.
DOI Google Scholar
55

Li, M.; Xu, C.; Ren, J. S.; Wang, E. B.; Qu, X. G. Photodegradation of β-sheet amyloid fibrils associated with Alzheimer's disease by using polyoxometalates as photocatalysts. Chem. Commun. 2013, 49, 11394-11396.
DOI Google Scholar
56

Li, M.; Liu, Z.; Ren, J. S.; Qu, X. G. Inhibition of metal- induced amyloid aggregation using light-responsive magnetic nanoparticle prochelator conjugates. Chem. Sci. 2012, 3, 868-873.
DOI Google Scholar
57

Rastogi, R. P.; Singh, S. P.; Häder, D. -P.; Sinha, R. P. Detection of reactive oxygen species (ROS) by the oxidant- sensing probe 2', 7'-dichlorodihydrofluorescein diacetate in the cyanobacterium Anabaena variabilis PCC 7937. Biochem. Biophys. Res. Commun. 2010, 397, 603-607.
DOI Google Scholar
58

Ahmed, M. H.; Keyesa, T. E.; Byrne, J. A. The photocatalytic inactivation effect of Ag-TiO2 on β-amyloid peptide (1-42). J. Photoch. Photobio. A: Chem. 2013, 254, 1-11.
DOI Google Scholar
59

Pramanik, D.; Ghosh, C.; Dey, S. G. Heme-Cu bound Aβ peptides: Spectroscopic characterization, reactivity, and relevance to Alzheimer's disease. J. Am. Chem. Soc. 2011, 133, 15545-15552.
DOI Google Scholar
60

Taniguchi, A.; Sasaki, D.; Shiohara, A.; Iwatsubo, T.; Tomita, T.; Sohma, Y.; Kanai, M. Attenuation of the aggregation and neurotoxicity of amyloid-β peptides by catalytic photooxygenation. Angew. Chem., Int. Ed. 2014, 53, 1382-1385.
DOI Google Scholar
61

D'Angelo, B.; Santucci, S.; Benedetti, E.; Di Loreto, S.; Phani, R.; Falone, S.; Amicarelli, F.; Cerù, M.; Cimini, A. Cerium oxide nanoparticles trigger neuronal survival in a human Alzheimer disease model by modulating BDNF pathway. Curr. Nanosci. 2009, 5, 167-176.
DOI Google Scholar
62

Li, M.; Shi, P.; Xu, C.; Ren, J. S.; Qu, X. G. Cerium oxide caged metal chelator: Anti-aggregation and anti-oxidation integrated H2O2-responsive controlled drug release for potential Alzheimer's disease treatment. Chem. Sci. 2013, 4, 2536-2542.
DOI Google Scholar
63

Harris, M. E.; Hensley, K.; Butterfield, D. A.; Leedle, R. A.; Carney, J. M. Direct evidence of oxidative injury produced by the Alzheimer's β-amyloid peptide (1-40) in cultured hippocampal neurons. Exp. Neurol. 1995, 131, 193-202.
DOI Google Scholar
64

Miranda, S.; Opazo, C.; Larrondo, L. F.; Muñoz, F. J.; Ruiz, F.; Leighton, F.; Inestrosa, N. C. The role of oxidative stress in the toxicity induced by amyloid beta-peptide in Alzheimer's disease. Prog. Neurobiol. 2000, 62, 633-648.
DOI Google Scholar
65

Liu, Y. L.; Ai, K. L.; Liu, J. H.; Yuan, Q. H.; He, Y. Y.; Lu, L. H. A high-performance ytterbium-based nanoparticulate contrast agent for in vivo X-ray computed tomography imaging. Angew. Chem., Int. Ed. 2012, 51, 1437-1442.
DOI Google Scholar
66

Liu, Z.; Pu, F.; Huang, S.; Yuan, Q. H.; Ren, J. S.; Qu, X. G. Long-circulating Gd2O3: Yb3+, Er3+ up-conversion nanoprobes as high-performance contrast agents for multi-modality imaging. Biomaterials 2013, 34, 1712-1721.
DOI Google Scholar
File
nr-9-8-2411_ESM.pdf (3.3 MB)
Publication history
Copyright
Acknowledgements

Publication history

Received: 05 February 2016
Revised: 25 April 2016
Accepted: 29 April 2016
Published: 01 June 2016
Issue date: August 2016

Copyright

© Tsinghua University Press and Springer-Verlag Berlin Heidelberg 2016

Acknowledgements

Acknowledgements

This work was supported by the National Basic Research Program of China (Nos. 2012CB720602 and 2011CB936004), and the National Natural Science Foundation of China (Nos. 21210002, 21431007, and 21533008).

Return