Monitoring of enzymatic proteolysis on a electroluminescent-CCD microchip platform using quantum dot-peptide substrates

Sensors and Actuators, B: Chemical

Volumn 139, Issue 1, 2009, Pages 13-21

  Sapsford, Kim E ^a   Farrell, Dorothy ^b   Sun, Steven ^a,c   Rasooly, Avraham ^a,d   Mattoussi, Hedi ^b   Medintz, Igor L ^b  

^a Engineering Laboratories   (United States)

^b NAVAL RESEARCH LABORATORY   (United States)

^c University of Marylandw Baltimore County   (United States)

^d NATIONAL CANCER INSTITUTE   (United States)

Author keywords

Biosensor; CCD; Electroluminescent excitation; FRET; Microfabricated device; Peptides; Protease sensor; Quantum dots; Resonance energy transfer; Trypsin

Indexed keywords

CCD; ELECTROLUMINESCENT EXCITATION; FRET; MICROFABRICATED DEVICE; PROTEASE SENSOR; QUANTUM DOTS; RESONANCE ENERGY TRANSFER; TRYPSIN;

AMINES; APPLICATIONS; BIOSENSORS; CHARGE COUPLED DEVICES; DIGITAL CAMERAS; ELECTROLUMINESCENCE; ENERGY TRANSFER; FLUORESCENCE; HYDROLYSIS; LIGHT EMISSION; MICROFABRICATION; MICROPROCESSOR CHIPS; MONITORING; OPTICAL WAVEGUIDES; PARAMETER ESTIMATION; PEPTIDES; RESONANCE; SUBSTRATES;

SEMICONDUCTOR QUANTUM DOTS;

EID: 67349174310     PISSN: 09254005     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.snb.2008.07.026     Document Type: Article

References (50)

1. Yager P., Edwards T., Fu E., Helton K., Nelson K., Tam M.R., and Weigl B.H. Microfluidic diagnostic technologies for global public health. Nature 442 (2006) 412-418
2. deMello A.J. Control and detection of chemical reactions in microfluidic systems. Nature 442 (2006) 394-402
3. Janshoff A., Galla H.J., and Steinem C. Piezoelectric mass-sensing devices as biosensors-An alternative to optical biosensors?. Angew. Chem. Int. Ed. 39 (2000) 4004-4032
4. Chin C.D., Linder V., and Sia S.K. Lab-on-a-chip devices for global health: Past studies and future opportunities. Lab Chip 7 (2007) 41-57
5. Sapsford K.E., Bradburne C., Detehanty J.B., and Medintz I.L. Sensors for detecting biological agents. Mater. Today 11 (2008) 38-49
6. Emrich C.A., Medintz I.L., Chu W.K., and Mathies R.A. Microfabricated two-dimensional electrophoresis device for differential protein expression profiling. Anal. Chem. 79 (2007) 7360-7366
7. Ristenpart W.D., Wan J., and Stone H.A. Enzymatic reactions in microfluidic devices: Michaelis-Menten kinetics. Anal. Chem. 80 (2008) 3270-3276
8. Medintz I., Uyeda H., Goldman E., and Mattoussi H. Quantum dot bioconjugates for imaging, labeling and sensing. Nat. Mater. 4 (2005) 435-446
9. Michalet X., Pinaud F.F., Bentolila L.A., Tsay J.M., Doose S., Li J.J., Sundaresan G., Wu A.M., Gambhir S.S., and Weiss S. Quantum dots for live cells, in vivo imaging, and diagnostics. Science 307 (2005) 538-544
10. Sapsford K.E., Berti L., and Medintz I.L. Materials for fluorescence resonance energy transfer: beyond traditional 'dye to dye' combinations. Angew. Chem. Int. Ed. 45 (2006) 4562-4588
11. Clapp A.R., Medintz I.L., and Mattoussi H. Förster resonance energy transfer investigations using quantum dot fluorophores. Chem. Phys. Chem. 7 (2005) 47-57
12. Clapp A.R., Medintz I.L., Mauro J.M., Fisher B.R., Bawendi M.G., and Mattoussi H. Fluorescence resonance energy transfer between quantum dot donors and dye-labeled protein acceptors. J. Am. Chem. Soc. 126 (2004) 301-310
13. Goldman E.R., Clapp A.R., Anderson G.P., Uyeda H.T., Mauro J.M., Medintz I.L., and Mattoussi H. Multiplexed toxin analysis using four colors of quantum dot fluororeagents. Anal. Chem. 76 (2004) 684-688
14. Clapp A.R., Medintz I.L., Uyeda H.T., Fisher B.R., Goldman E.R., Bawendi M.G., and Mattoussi H. Quantum dot-based multiplexed fluorescence resonance energy transfer. J. Am. Chem. Soc. 127 (2005) 18212-18221
15. Puente X.S., Sanchez L.M., Overall C.M., and Lopez-Otin C. Human and mouse proteases: A comparative genomic approach. Nat. Rev. Genet. 4 (2003) 544-558
16. Vihinen P., Ala-Aho R., and Kahari V.M. Matrix metalloproteinases as therapeutic targets in cancer. Curr. Cancer Drug. Targets 5 (2005) 203-220
17. Ala-Aho R., and Kahari V.M. Collagenases in cancer. Biochimie 87 (2005) 273-286
18. Richard I. The genetic and molecular bases of monogenic disorders affecting proteolytic systems. J. Med. Genet. 42 (2005) 529-539
19. Wu Y.M., Wang X.Y., Liu X., and Wang Y.F. Data-mining approaches reveal hidden families of proteases in the genome of malaria parasite. Genome Res. 13 (2003) 601-616
20. Shao F., Merritt P.M., Bao Z.Q., Innes R.W., and Dixon J.E. A Yersinia effector and a pseudomonas avirulence protein define a family of cysteine proteases functioning in bacterial pathogenesis. Cell 109 (2002) 575-588
21. Anand K., Ziebuhr J., Wadhwani P., Mesters J.R., and Hilgenfeld R. Coronavirus main proteinase (3CL(pro)) structure: basis for design of anti-SARS drugs. Science 300 (2003) 1763-1767
22. Schmidt J.J., and Stafford R.G. Fluorigenic substrates for the protease activities of botulinum neurotoxins, serotypes A, B, and F. Appl. Environ. Microbiol. 69 (2003) 297-303
23. Taliani M., Bianchi E., Narjes F., Fossatelli M., Urbani A., Steinkuhler C., DeFrancesco R., and Pessi A. A continuous assay of hepatitis C virus protease based on resonance energy transfer depsipeptide substrates. Anal. Biochem. 240 (1996) 60-67
24. Grahn S., Ullmann D., and Jakubke H.D. Design and synthesis of fluorogenic trypsin peptide substrates based on resonance energy transfer. Anal. Biochem. 265 (1998) 225-231
25. Grant S.A., Weilbaecher C., and Lichlyter D. Development of a protease biosensor utilizing silica nanobeads. Sens. Actuators B-Chem. 121 (2007) 482-489
26. Eggeling C., Kask P., Winkler D., and Jager S. Rapid analysis of Forster resonance energy transfer by two-color global fluorescence correlation spectroscopy: Trypsin proteinase reaction. Biophys. J. 89 (2005) 605-618
27. Matayoshi E.D., Wang G.T., Krafft G.A., and Erickson J. Novel fluorogenic substrates for assaying retroviral proteases by resonance energy transfer. Science 247 (1990) 954-958
28. Medintz I.L., Clapp A.R., Brunel F.M., Tiefenbrunn T., Uyeda H.T., Chang E.L., Deschamps J.R., Dawson P.E., and Mattoussi H. Proteolytic activity monitored by fluorescence resonance energy transfer through quantum-dot-peptide conjugates. Nat. Mater. 5 (2006) 581-589
29. Murray C.B., Norris D.J., and Bawendi M.G. Synthesis and characterization of nearly monodisperse CdE (E = sulfur, selenium, tellurium) semiconductor nanocrystallites. J. Am. Chem. Soc. 115 (1993) 8706-8715
30. Qu L., Peng Z.A., and Peng X. Alternative routes toward high quality CdSe nanocrystals. Nano Lett. 1 (2001) 333-337
31. Dabbousi B.O., Rodriguez-Viejo J., Mikulec F.V., Heine J.R., Mattoussi H., Ober R., Jensen K.F., and Bawendi M.G. (CdSe)ZnS core-shell quantum dots: synthesis and optical and structural characterization of a size series of highly luminescent materials. J. Phys. Chem. B. 101 (1997) 9463-9475
32. Mattoussi H., Mauro J.M., Goldman E.R., Anderson G.P., Sundar V.C., Mikulec F.V., and Bawendi M.G. Self-assembly of CdSe-ZnS quantum dot bioconjugates using an engineered recombinant protein. J. Am. Chem. Soc. 122 (2000) 12142-12150
33. Uyeda H.T., Medintz I.L., Jaiswal J.K., Simon S.M., and Mattoussi H. Synthesis of compact multidentate ligands to prepare stable hydrophilic quantum dot fluorophores. J. Am. Chem. Soc. 127 (2005) 3870-3878
34. Susumu K., Uyeda H.T., Medintz I.L., Pons T., Delehanty J.B., and Mattoussi H. Enhancing the stability and biological functionalities of quantum dots via compact multifunctional ligands. J. Am. Chem. Soc. 129 (2007) 13987-13996
35. Lakowicz J.R. Principles of Fluorescence Spectroscopy (2006), Springer, New York
36. Pons T., Medintz I.L., Wang X., English D.S., and Mattoussi H. Solution-phase single quantum dot fluorescence resonant energy transfer sensing. J. Am. Chem. Soc. 128 (2006) 15324-15331
37. Harris D.A. Spectrophotometric assays (1987), IRL Press, Washington DC
38. Dixon M. The determination of enzyme inhibitor constants. Biochem. J. 55 (1953) 170-171
39. Bowden A.C. Fundamentals of Enzyme Kinetics (1995), Portland Press Limited, London
40. Segel I.H. Enzyme Kinetics: Behavior and Analysis of Rapid Equilibrium and Steady-State Enzyme Systems (1993), Wiley-Interscience, Hoboken, NJ
41. Sapsford K.E., Pons T., Medintz I.L., Higashiya S., Brunel F.M., Dawson P.E., and Mattoussi H. Kinetics of metal-affinity driven self-assembly between proteins or peptides and CdSe-ZnS quantum dots. J. Phys. Chem. C 111 (2007) 11528-11538
42. K.E. Sapsford, S. Sun, J. Francis, S. Sharma, Y. Kostov, A. Rasooly, Using spatial electroluminescent excitation for measuring botulinum neurotoxin A activity, Biosensors and Bioelectronics (in press), doi:10.1016/j.bios.2008.06.018.
43. Malesevic M., Majer Z., Vass E., Huber T., Strijowski U., Hollosi M., and Sewald N. Spectroscopic detection of pseudo-turns in homodetic cyclic penta- and hexapeptides comprising beta-homoproline. Int. J. Peptide Res. Ther. 12 (2006) 165-177
44. Shi L., Rosenzweig N., and Rosenzweig Z. Luminescent quantum dots fluorescence resonance energy transfer-based probes for enzymatic activity and enzyme Inhibitors. Anal. Chem. 79 (2007) 208-214
45. Van der Plancken I., Van Remoortere M., Van Loey A., and Hendrickx M.E. Trypsin inhibition activity of heat-denatured ovomucoid: A kinetic study. Biotechnol. Prog. 20 (2004) 82-86
46. Zhou J.M., Liu C., and Tsou C.L. Kinetics of trypsin inhibition by its specific inhibitors. Biochemistry 28 (1989) 1070-1076
47. Lineweaver H., and Murray C.W. Identification of the trypsin inhibitor of egg white with ovomucoid. J. Biol. Chem. 171 (1947) 565-581
48. Xu C.J., Xing B.G., and Rao H.H. A self-assembled quantum dot probe for detecting beta-lactamase activity. Biochem. Biophys. Res. Commun. 344 (2006) 931-935
49. Goldman E., Medintz I., Whitley J., Hayhurst A., Clapp A., Uyeda H., Deschamps J., Lassman M., and Mattoussi H. A hybrid quantum dot-antibody fragment fluorescence resonance energy transfer-based TNT sensor. J. Am. Chem. Soc. 127 (2005) 6744-6751
50. Sapsford K.E., Pons T., Medintz I.L., and Mattoussi H. Biosensing with luminescent semiconductor quantum dots. Sensors 6 (2006) 925-953