Immune-independent and label-free fluorescent assay for Cystatin C detection based on protein-stabilized Au nanoclusters

Biosensors and Bioelectronics

Volumn 41, Issue 1, 2013, Pages 256-261

  Lin, Hui ^a   Li, Lijun ^a   Lei, Chunyang ^a   Xu, Xiahong ^a   Nie, Zhou ^a   Guo, Manli ^a   Huang, Yan ^a   Yao, Shouzhuo ^a  

^a HUNAN UNIVERSITY   (China)

Author keywords

Au nanoclusters; Cystatin C; Fluorescence probe; Papain

Indexed keywords

AU NANOCLUSTERS; CLINICAL SAMPLES; CYSTATINS; CYSTEINE PROTEASE ACTIVITY; CYSTEINE PROTEASE INHIBITORS; DETECTION LIMITS; FLUORESCENCE PROBES; FLUORESCENT ASSAYS; FLUORESCENT PROBES; GLOMERULAR FILTRATION RATE; HUMAN BODIES; LABEL FREE; OPTIMIZED CONDITIONS; PAPAIN; PERCENTAGE RECOVERY; QUENCHING MECHANISMS; RELATIVE STANDARD DEVIATIONS; SCAFFOLD DEGRADATION; SDS-PAGE; SPIKED URINE SAMPLES; TRANSMISSION ELECTRON MICROSCOPE;

AMINO ACIDS; NANOCLUSTERS; PHOTOELECTRONS; PROTEINS; TRANSMISSION ELECTRON MICROSCOPY; X RAY PHOTOELECTRON SPECTROSCOPY;

FLUORESCENCE;

BOVINE SERUM ALBUMIN; CYSTATIN C; GOLD NANOPARTICLE; PAPAIN; GOLD; METAL NANOPARTICLE; HUMAN SERUM ALBUMIN;

ABSORPTION SPECTROSCOPY; ACCURACY; ARTICLE; CONCENTRATION (PARAMETERS); CONTROLLED STUDY; COST EFFECTIVENESS ANALYSIS; ENZYME ACTIVITY; ENZYME INHIBITION; FLUORESCENCE ANALYSIS; HUMAN; INTERMETHOD COMPARISON; LIGHT SCATTERING; LIMIT OF DETECTION; NANOPROBE; NANOSENSOR; PARTICLE SIZE; POLYACRYLAMIDE GEL ELECTROPHORESIS; PROCESS OPTIMIZATION; PRODUCT RECOVERY; PROTEIN ANALYSIS; PROTEIN DEGRADATION; PROTEIN STABILITY; SENSITIVITY AND SPECIFICITY; TRANSMISSION ELECTRON MICROSCOPY; URINALYSIS; X RAY PHOTOELECTRON SPECTROSCOPY; CHEMISTRY; EQUIPMENT; EQUIPMENT DESIGN; EQUIPMENT FAILURE; GENETIC PROCEDURES; IMMUNOASSAY; NANOTECHNOLOGY; REPRODUCIBILITY; SPECTROFLUOROMETRY; STAINING; ASSAY; ENZYME SPECIFICITY; IMMUNE INDEPENDENT ASSAY; LABEL FREE FLUORESCENT ASSAY; NANOANALYSIS; PROTEIN DETERMINATION; PROTEIN INTERACTION; STATISTICAL ANALYSIS;

BIOSENSING TECHNIQUES; CYSTATIN C; EQUIPMENT DESIGN; EQUIPMENT FAILURE ANALYSIS; GOLD; IMMUNOASSAY; METAL NANOPARTICLES; NANOTECHNOLOGY; PROTEIN INTERACTION MAPPING; REPRODUCIBILITY OF RESULTS; SENSITIVITY AND SPECIFICITY; SERUM ALBUMIN, BOVINE; SPECTROMETRY, FLUORESCENCE; STAINING AND LABELING;

EID: 84870835096     PISSN: 09565663     EISSN: 18734235     Source Type: Journal    
DOI: 10.1016/j.bios.2012.08.030     Document Type: Article

References (45)

1. Abrahamson M., Alvarez-Fernandez M., Nathanson C.M. Biochemical Society Symposium 2003, 70:179-199.
2. Anastasi A., Brown M.A., Kembhavi A.A., Nicklin M.J.H., Sayers C.A., Sunter D.C., Barrett A.J. The Biochemical Journal 1983, 211:129-138.
3. Bökenkamp A., Domanetzki M., Zinck R., Schumann G., Byrd D., Brodehl J. Pediatrics 1998, 101:875-881.
4. Bigioni T.P., Whetten R.L., Dag Ö. The Journal of Physical Chemistry B 2000, 104:6983-6986.
5. Cai L., Borowiec J., Xu S., Han W., Venge P. Clinica Chimica Acta 2009, 403:121-125.
6. Chen W., Tu X., Guo X. Chemical Communications 2009, 13:1736-1738.
7. Collé A., Tavera C., Prévot D., Leung-Tack J., Thomas Y., Manuel Y., Benveniste J., Leibowitch J. Journal of Immunoassay 1992, 13:47-60.
8. Dickerson M.B., Sandhage K.H., Naik R.R. Chemical Reviews 2008, 108:4935-4978.
9. Filler G., Bökenkamp A., Hofmann W., Le Bricon T., Martínez-Brú C., Grubb A. Clinical Biochemistry 2005, 38:1-8.
10. Finney H., Newman D.J., Gruber W., Merle P., Price C.P. Clinical Chemistry 1997, 43:1016-1022.
11. Fliser D., Ritz E. American Journal of Kidney Diseases 2001, 37:79-83.
12. Fukuzumi S., Endo Y., Kashiwagi Y., Araki Y., Ito O., Imahori H. The Journal of Physical Chemistry B 2003, 107:11979-11986.
13. Gorodkiewicz E. Protein and Peptide Letters 2011, 14:443-445.
14. Gorodkiewicz E., Luszczyn J. Protein and Peptide Letters 2011, 18:23-29.
15. Hu L., Han S., Parveen S., Yuan Y., Zhang L., Xu G. Biosensors & Bioelectronics 2012, 32:297-299.
16. Huang T., Murray R.W. The Journal of Physical Chemistry B 2001, 105:12498-12502.
17. Jiborn T., Abrahamson M., Wallin H., Malm J., Lundwall A., Gadaleanu V., Abrahamsson P.A., Bjartell A. Journal of Andrology 2004, 25:564-572.
18. Jin L., Shang L., Guo S., Fang Y., Wen D., Wang L., Yin J., Dong S. Biosensors & Bioelectronics 2011, 26:1965-1969.
19. Koyner J.L., Bennett M.R., Worcester E.M., Ma Q., Raman J., Jeevanandam V., Kasza K.E., Connor M.F.O., Konczal D.J., Trevino S., Devarajan P., Murray P.T. Kidney International 2008, 74:1059-1069.
20. Kundu S., Maheshwari V., Saraf R.F. Langmuir 2007, 24:551-555.
21. Kyhse-Andersen J., Schmidt C., Nordin G., Andersson B., Nilsson-Ehle P. Clinical Chemistry 1994, 40:1921-1926.
22. LaLonde J.M., Zhao B., Smith W.W., Janson C.A., DesJarlais R.L., Tomaszek T.A., Carr T.J., Thompson S.K., Oh H.J., Yamashita D.S., Veber D.F., Abdel-Meguid S.S. Journal of Medicinal Chemistry 1998, 41:4567-4576.
23. Lin C.A.J., Yang T.Y., Lee C.H., Huang S.H., Sperling R.A., Zanella M., Li J.K., Shen J.L., Wang H.H., Yeh H.-I., Parak W.J., Chang W.H. ACS Nano 2009, 3:395-401.
24. Lin C.A.J., Lee C.H. Journal of Medical and Biological Engineering 2009, 29:276-283.
25. Liu C.L., Wu H.T., Hsiao Y.H., Lai C.W., Shih C.W., Peng Y.K., Tang K.C., Chang H.W., Chien Y.C., Hsiao J.K., Cheng J.T., Chou P.T. Angewandte Chemie-International Edition 2011, 50:7056-7060.
26. Liu Y., Ai K., Cheng X., Huo L., Lu L. Advanced Functional Materials 2010, 20:951-956.
27. Muhammed M.A.H., Pradeep T., Demchenko A.P. Advanced Fluorescence Reporters in Chemistry and Biology 2010, II(9):333-354.
28. Nagai A., Murakawa Y., Terashima M., Shimode K., Umegae N., Kobayashi S. Neurology 2000, 55:1828-1832.
29. Negishi Y., Takasugi Y., Sato S., Yao H., Kimura K., Tsukuda T. Journal of the American Chemical Society 2004, 126:6518-6519.
30. Newman D.J., Thakkar H., Edwards R.G., Wilkie M., White T., Grubb A.O., Price C.P. Kidney International 1995, 47:312-318.
31. Otto H.H., Schirmeister T. Chemical Reviews 1997, 97:133-172.
32. Rawlings N.D., Barrett A.J., Alan J.B. Methods in Enzymology 1994, 244:461-486.
33. Sangeetha K., Abraham T.E. Journal of Molecular Catalysis B-Enzymatic 2006, 38:171-177.
34. Schipper R., Loof A., de Groot J., Harthoorn L., Dransfield E., van Heerde W. Journal of Chromatography B 2007, 847:45-53.
35. Smith E.L., Kimmel J.R., Brown D.M. The Journal of Biological Chemistry 1954, 207:533-549.
36. Shlipak M.G., Sarnak M.J., Katz R. New England Journal of Medicine 2005, 352:2049-2060.
37. Tang Z., Xu B., Wu B., Germann M.W., Wang G. Journal of the American Chemical Society 2010, 132:3367-3374.
38. Travis J., Potempa J., Maeda H. Trends in Microbiology 1995, 3:405-407.
39. Turner N.H., Schreifels J.A. Analytical Chemistry 2000, 72:99-110.
40. Wang Y., Cui Y., Zhao Y., Liu R., Sun Z., Li W., Gao X. Chemical Communications 2012, 48:871-873.
41. Wu X., He X., Wang K., Xie C., Zhou B., Qing Z. Nanoscale 2010, 2:2244-2249.
42. Wu Z., Jin R. Nano letters 2010, 10:2568-2573.
43. Xie J., Zheng Y., Ying J.Y. Chemical Communications 2010, 46:961-963.
44. Xie J., Zheng Y., Ying J.Y. Journal of the American Chemical Society 2009, 131:888-889.
45. Yano M., Hirai K., Naito Z., Yokoyama M., Ishiwata T., Shiraki Y., Inokuchi M., Asano G. Surgery Today 2001, 31:385-389.