A new methodology for monitoring the activity of cdMMP-12 anchored and freeze-dried on Au (111)(359 views) Grasso G, Fragai M, Rizzarelli E, Spoto G, Yeo KJ
Journal Of The American Society For Mass Spectrometry (ISSN: 1044-0305), 2007 May; 18(5): 961-969.
Consorzio Interuniversitario di Ricerca in Chimica dei Metalli nei Sistemi Biologici, Bari, Italy.
Magnetic Resonance Center (CERM), University of Florence, Sesto Fiorentino, Italy
Dipartimento di Scienze Chimiche, Università di Catania, Catania, Italy
References: (2006) Enzyme Assays: High-throughput Screening, Genetic Selection and Fingerprinting, , Reymond J.L. (Ed), Wiley-VCH, New Yor
Min, D.-H., Tang, W.-J., Mrksich, M., Chemical Screening by Mass Spectrometry to Identify Inhibitors of Anthrax Lethal Factor (2004) Nat. Biotechnol., 22, pp. 717-723
Su, J., Bringer, M.R., Ismagilov, R.F., Mrksich, M., Combining Microfluidic Networks and Peptide Arrays for Multi-enzyme Assays (2005) J. Am. Chem. Soc., 127, pp. 7280-7281
Min, D.H., Yeo, W.S., Mrksich, M., A Method for Connecting Solution-phase Enzyme Activity Assays with Immobilized Format Analysis by Mass Spectrometry (2004) Anal. Chem., 76, pp. 3923-3929
Shen, Z., Go, E.P., Gamez, A., Apon, J.V., Fokin, V., Greig, M., Ventura, M., Siuzdak, G., A Mass Spectrometry Plate Reader: Monitoring Enzyme Activity and Inhibition with a Desorption/Ionization on Silicon (DIOS) Platform (2004) Chem. Biol. Chem., 5, pp. 921-927
Min, D., Mrksich, M., Profiling Kinase Activities by Using a Peptide Chip and Mass Spectrometry (2004) Angew. Chem. Int. Ed., 43, pp. 5973-5977
Babiak, P., Reymond, J., A High-throughput, Low-volume Enzyme Assay on Solid Support (2005) Anal. Chem., 77, pp. 373-377
Huber, W., Hoffman, F., A New Strategy for Improved Secondary Screening and Lead Optimization Using High-resolution SPR Characterization of Compound-Target Interactions (2005) J. Mol. Recogn., 18, pp. 273-281
Nedelkov, D., Nelson, R.W., Surface Plasmon Resonance Mass Spectrometry for Protein Analysis (2006) Methods Mol. Biol., 328, pp. 131-139
Borch, J., Roepstorff, P., Screening for Enzyme Inhibitors by Surface Plasmon Resonance Combined with Mass Spectrometry (2004) Anal. Chem., 76, pp. 5243-5248
Massova, I., Kotra, L.P., Fridman, R., Mobashery, S., Matrix Metalloproteinases: Structures, Evolution, and Diversification (1998) FASEB J., 12, pp. 1075-1095
Coussens, L.M., Werb, Z., Matrix Metalloproteinases and the Development of Cancer (1996) Chem. Biol., 3, pp. 895-904
Ramsey, K.H., Sigar, I.M., Schripsema, J.H., Shaba, N., Cohoon, K.P., Expression of Matrix Metalloproteinases Subsequent to Urogenital Chlamydia muridarum Infection of Mice (2005) Infect. Immun., 73, pp. 6962-6973
Koivunen, E., Arap, W., Valtanen, H., Rainisalo, A., Medina, O.P., Heikkilä, P., Kantor, C., Pasqualini, R., Tumor Targeting with a Selective Gelatinase Inhibitor (1999) Nat. Biotechnol., 17, pp. 768-774
Farkas, E., Katz, Y., Bhusare, S., Reich, R., Röschenthaler, G., Königsmann, M., Breuer, E., Carbamoylphosphonate-based Matrix Metalloproteinase (MMP) Inhibitor Metal Complexes-Solution Studies and Stability Constants. Towards a Zinc-selective Binding Group (2004) J. Biol. Inorg. Chem., 9, pp. 307-315
Dublanchet, A., Ducrot, P., Andrianjara, C., O'Gara, M., Morales, R., Compere, D., Denis, A., Tertre, A., Structure-based Design and Synthesis of Novel Non-zinc Chelating MMP-12 Inhibitors (2005) Bioorg. Med. Chem. Lett., 15, pp. 3787-3790
Dive, V., Andarawewa, K.L., Boulay, A., Matziari, M., Beau, F., Guerin, E., Rousseau, B., Rio, M., Dosing and Scheduling Influence the Antitumor Efficacy of a Phosphinic Peptide Inhibitor of Matrix Metalloproteinases (2005) Int. J. Cancer, 113, pp. 775-781
Weingarten, H., Feder, J., Spectrophotometric Assay for Vertebrate Collagenase (1985) Anal. Biochem., 147, pp. 437-440
Beekman, B., Drijfhout, J.W., Bloemhoff, W., Ronday, H.K., Tak, P.P., Koppele, J.M., Convenient Fluorometric Assay for Matrix Metalloproteinase Activity and Its Application in Biological Media (1996) FEBS Lett., 390, pp. 221-225
Liu, Y., Kati, W., Chen, C., Tripathy, R., Molla, A., Kohlbreuner, W., Use of a Fluorescence Plate Reader for Measuring Kinetic Parameters with Inner Filter Effect Correction (1999) Anal. Biochem., 267, pp. 331-335
Lauer-Fields, J.L., Nagase, H., Fields, G.B., Development of a Solid-phase Assay for Analysis of Matrix Metalloproteinase Activity (2004) J. Biomol. Technol., 15, pp. 305-316
Didraga, M., Barroso, B., Bischoff, R., Recent Developments in Proteoglycan Purification and Analysis (2006) Curr. Pharm. Anal., 2, pp. 323-337
Banci, L., Bertini, I., Calderone, V., Ciofi-Baffoni, S., Mangani, S., Martinelli, M., Palumaa, P., Wang, S., A Hint for the Function of Human Sco1 from Different Structures (2006) Proc. Natl. Acad. Sci. U.S.A., 103, pp. 8595-8600
Devreese, B., Van Beeumen, J., The Important Contribution of High Precision Mass Spectrometric Methods in the Study of the Structure-Function Relationship of Proteins and Enzymes (1998) Analyst, 123, pp. 2457-2461
Bothner, B., Chavez, R., Wei, J., Strupp, C., Phung, Q., Schneemann, A., Siuzdak, G., Monitoring Enzyme Catalysis with Mass Spectrometry (2000) J. Biol. Chem., 275, pp. 13455-13459
Somsen, G.W., Mol, R., de Jong, G.J., On-line Micellar Electrokinetic Chromatography-Mass Spectrometry: Feasibility of Direct Introduction of Non-volatile Buffer and Surfactant into the Electrospray Interface (2003) J. Chromatogr. A, 1000, pp. 953-961
Ong, S., Mann, M., Mass-spectrometry Based Proteomics Turns Quantitative (2005) Nat. Chem. Biol., 1, pp. 252-262
Su, J., Mrksich, M., Using Mass Spectrometry to Characterize Self-assembled Monolayers Presenting Peptides, Proteins, and Carbohydrates (2002) Angew. Chem. Int. Ed., 41, pp. 4715-4718
Olson, M.W., Gervasi, D.C., Mobashery, S., Fridman, R., Kinetic Analysis of the Binding of Human Matrix Metalloproteinase-2 and -9 to Tissue Inhibitor of Metalloproteinase (TIMP)-1 and TIMP-2 (1997) J. Biol. Chem., 272, pp. 29975-29983
Pieper-Fürst, U., Kleuser, U., Stöcklein, W.F.M., Warsinke, A., Scheller, F.W., Detection of Subpicomolar Concentrations of Human Matrix Metalloproteinase-2 by an Optical Biosensor (2004) Anal. Biochem., 332, pp. 160-167
Grasso, G., D'Agata, R., Rizzarelli, E., Spoto, G., Picardi, A., Romanelli, A., Fragai, M., Yeo, K.J., Activity of Anchored Human Matrix Metalloproteinase-1 Catalytic Domain on Au (111) Surfaces Monitored by ESI-MS (2005) J. Mass Spectrom., 40, pp. 1565-1571
Grasso, G., Fragai, M., Rizzarelli, E., Spoto, G., Kwon, J.Y., In Situ AP/MALDI-MS Characterization of Anchored Matrix Metalloproteinases (2006) J. Mass Spectrom., 41, pp. 1561-1569
Weingarten, H., Martin, R., Feder, J., Synthetic Substrates of Vertebrate Collagenase (1985) Biochemistry, 24, pp. 6730-6734
MacPherson, L.J., Bayburt, E.K., Capparelli, M.P., Carroll, B.J., Goldstein, R., Justice, M.R., Zhu, L., Parker, D.T., Discovery of CGS 27023A, a Non-peptidic, Potent, and Orally Active Stromelysin Inhibitor That Blocks Cartilage Degradation in Rabbits (1997) J. Med. Chem., 40, pp. 2525-2532
Lide, D.R., (1990) Handbook of Chemistry and Physics. 71st ed., , CRC Press, Boston
Jung, L.S., Campbell, C.T., Chinowsky, T.M., Mar, M.N., Yee, S.S., Quantitative Interpretation of the Response of Surface Plasmon Resonance Sensors to Adsorbed Films (1998) Langmuir, 14, pp. 5636-5648
Wang, X., Sakuma, T., Asafu-Adjaye, E., Shiu, G.K., Determination of Ginsenosides in Plant Extracts from Panax ginseng and Panax quinquefolius L. by LC/MS/MS (1999) Anal. Chem., 71, pp. 1579-1584
Mauri, P., Migliazza, B., Pietta, P., Liquid Chromatography/Electrospray Mass Spectrometry of Bioactive Terpenoids in Ginkgo biloba L (1999) J. Mass Spectrom., 34, pp. 1361-1367
Pi, N., Leary, J.A., Determination of Enzyme/Substrate Specificity Constants Using a Multiple Substrate ESI-MS Assay (2004) J. Am. Soc. Mass Spectrom., 15, pp. 233-243
Gao, H., Leary, J.A., Multiplex Inhibitor Screening and Kinetic Constant Determinations for Yeast Hexokinase Using Mass Spectrometry Based Assays (2003) J. Am. Soc. Mass Spectrom., 14, pp. 173-181
Pi, N., Armstrong, J.I., Bertozzi, C.R., Leary, J.A., Kinetic Analysis of NodST Sulfotransferase Using an Electrospray Ionization Mass Spectrometry Assay (2002) Biochemistry, 41, pp. 13283-13288
Iavarone, A.T., Udekwu, O.A., Williams, E.R., Buffer Loading for Counteracting Metal Salt-induced Signal Suppression in Electrospray Ionization (2004) Anal. Chem., 76, pp. 3944-3950
Wang, G., Cole, R.B., Solvation Energy and Gas-phase Stability Influences on Alkali Metal Cluster Ion Formation in Electrospray Ionization Mass Spectrometry (1998) Anal. Chem., 70, pp. 873-881
Blades, A.T., Peschke, M., Verkerk, U.H., Kebarle, P., Hydration Energies in the Gas Phase of Select (MX)mM+ Ions, Where M+ = Na+, K+, Rb+, Cs+, NH4 + and X- = F-, Cl-, Br-, I-, NO2 -, NO3 -. Observed Magic Numbers of (MX)mM+ Ions (2004) J. Am. Chem. Soc., 126, pp. 11995-12003
Hao, C., March, R.E., Croley, T.R., Smith, J.C., Rafferty, S.P., Electrospray Ionization Tandem Mass Spectrometric Study of Salt Cluster Ions. Part 1-Investigations of Alkali Metal Chloride and Sodium Salt Cluster Ions (2001) J. Mass Spectrom., 36, pp. 79-96
Zhang, D., Cooks, R.G., Doubly Charged Ions [(NaCl)m(Na)2]2+: Magic Numbers, Dissociation, and Structure (2000) Int. J. Mass Spectrom., 195-196, pp. 667-684
Neumann, U., Kubota, H., Frei, K., Ganu, V., Leppert, D., Characterization of Mca-Lys-Pro-Leu-Gly-Leu-Dppa-Ala-Arg-NH2, a Fluorogenic Substrate with Increased Specificity Constants for Collagenases and Tumor Necrosis Factor Converting Enzyme (2004) Anal. Biochem., 328, pp. 166-173
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Min, D. -H., Tang, W. -J., Mrksich, M., Chemical Screening by Mass Spectrometry to Identify Inhibitors of Anthrax Lethal Factor (2004) Nat. Biotechnol., 22, pp. 717-723
Min, D. H., Yeo, W. S., Mrksich, M., A Method for Connecting Solution-phase Enzyme Activity Assays with Immobilized Format Analysis by Mass Spectrometry (2004) Anal. Chem., 76, pp. 3923-3929
Shen, Z., Go, E. P., Gamez, A., Apon, J. V., Fokin, V., Greig, M., Ventura, M., Siuzdak, G., A Mass Spectrometry Plate Reader: Monitoring Enzyme Activity and Inhibition with a Desorption/Ionization on Silicon (DIOS) Platform (2004) Chem. Biol. Chem., 5, pp. 921-927
Coussens, L. M., Werb, Z., Matrix Metalloproteinases and the Development of Cancer (1996) Chem. Biol., 3, pp. 895-904
Ramsey, K. H., Sigar, I. M., Schripsema, J. H., Shaba, N., Cohoon, K. P., Expression of Matrix Metalloproteinases Subsequent to Urogenital Chlamydia muridarum Infection of Mice (2005) Infect. Immun., 73, pp. 6962-6973
Lauer-Fields, J. L., Nagase, H., Fields, G. B., Development of a Solid-phase Assay for Analysis of Matrix Metalloproteinase Activity (2004) J. Biomol. Technol., 15, pp. 305-316
Somsen, G. W., Mol, R., de Jong, G. J., On-line Micellar Electrokinetic Chromatography-Mass Spectrometry: Feasibility of Direct Introduction of Non-volatile Buffer and Surfactant into the Electrospray Interface (2003) J. Chromatogr. A, 1000, pp. 953-961
Olson, M. W., Gervasi, D. C., Mobashery, S., Fridman, R., Kinetic Analysis of the Binding of Human Matrix Metalloproteinase-2 and -9 to Tissue Inhibitor of Metalloproteinase (TIMP) -1 and TIMP-2 (1997) J. Biol. Chem., 272, pp. 29975-29983
Pieper-F rst, U., Kleuser, U., St cklein, W. F. M., Warsinke, A., Scheller, F. W., Detection of Subpicomolar Concentrations of Human Matrix Metalloproteinase-2 by an Optical Biosensor (2004) Anal. Biochem., 332, pp. 160-167
MacPherson, L. J., Bayburt, E. K., Capparelli, M. P., Carroll, B. J., Goldstein, R., Justice, M. R., Zhu, L., Parker, D. T., Discovery of CGS 27023A, a Non-peptidic, Potent, and Orally Active Stromelysin Inhibitor That Blocks Cartilage Degradation in Rabbits (1997) J. Med. Chem., 40, pp. 2525-2532
Lide, D. R., (1990) Handbook of Chemistry and Physics. 71st ed., , CRC Press, Boston
Jung, L. S., Campbell, C. T., Chinowsky, T. M., Mar, M. N., Yee, S. S., Quantitative Interpretation of the Response of Surface Plasmon Resonance Sensors to Adsorbed Films (1998) Langmuir, 14, pp. 5636-5648
Pi, N., Leary, J. A., Determination of Enzyme/Substrate Specificity Constants Using a Multiple Substrate ESI-MS Assay (2004) J. Am. Soc. Mass Spectrom., 15, pp. 233-243
Gao, H., Leary, J. A., Multiplex Inhibitor Screening and Kinetic Constant Determinations for Yeast Hexokinase Using Mass Spectrometry Based Assays (2003) J. Am. Soc. Mass Spectrom., 14, pp. 173-181
Iavarone, A. T., Udekwu, O. A., Williams, E. R., Buffer Loading for Counteracting Metal Salt-induced Signal Suppression in Electrospray Ionization (2004) Anal. Chem., 76, pp. 3944-3950
Wang, G., Cole, R. B., Solvation Energy and Gas-phase Stability Influences on Alkali Metal Cluster Ion Formation in Electrospray Ionization Mass Spectrometry (1998) Anal. Chem., 70, pp. 873-881
Blades, A. T., Peschke, M., Verkerk, U. H., Kebarle, P., Hydration Energies in the Gas Phase of Select (MX) mM+ Ions, Where M+ = Na+, K+, Rb+, Cs+, NH4 + and X- = F-, Cl-, Br-, I-, NO2 -, NO3 -. Observed Magic Numbers of (MX) mM+ Ions (2004) J. Am. Chem. Soc., 126, pp. 11995-12003
Hao, C., March, R. E., Croley, T. R., Smith, J. C., Rafferty, S. P., Electrospray Ionization Tandem Mass Spectrometric Study of Salt Cluster Ions. Part 1-Investigations of Alkali Metal Chloride and Sodium Salt Cluster Ions (2001) J. Mass Spectrom., 36, pp. 79-96
Clark, I. M., Mitchell, R. E., Powell, L. K., Bigg, H. F., Cawston, T. E., O'Hare, M. C., Recombinant Porcine Collagenase: Purification and Autolysis (1995) Arch. Biochem. Biophys., 316, pp. 123-127
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A new methodology for monitoring the activity of cdMMP-12 anchored and freeze-dried on Au (111)
Matrix metalloproteinases (MMPs) are cell-secreted soluble and membrane-tethered enzymes that are capable of degrading extracellular matrix proteins, but also can process a number of bioactive molecules. They are involved in the cleavage of cell surface receptors, but are also thought to play a major role on cell behaviors as well as in diverse physiological and pathological processes, including embryonic development, wound repair, inflammatory diseases, and cancer. For these reasons, it is obvious that a control over MMPs activity is highly desirable. Consequently, the frantic search for new inhibitors has been coupled to the development of high-throughput methods able to rapidly screen the effect of possible MMP inhibitors on the activity of these enzymes. In this scenario, solid-state-based methods play a major role because of their compatibility with array formats that are able to extract more information from smaller sample volumes and offer some important advantages that are not available in the standard solution assays. In this work, the catalytic domain of MMP-12 was immobilized on a gold substrate and the surface coverage was measured by FT-SPR experiments. A new experimental procedure was developed to freeze-dry the anchored molecules and their activity was measured by ESI-MS. The kinetics parameters obtained for the immobilized enzyme are in good accordance with those reported for similar systems in solution. Inhibition of the immobilized molecules was also carried out, demonstrating the applicability of the method for rapid screening of MMP inhibitors.
A new methodology for monitoring the activity of cdMMP-12 anchored and freeze-dried on Au (111)