Activity of anchored human matrix metalloproteinase-1 catalytic domain on Au(111) surfaces monitored by ESI-MS (999 views)
J Mass Spectrom (ISSN: 1076-5174, 1096-9888), 2005 Dec; 40(12): 1565-1571.
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Paper type: Journal Article,
Impact factor: 3.574, 5-year impact factor: 3.017
Url: http://www.scopus.com/inward/record.url?eid=2-s2.0-30044445496&partnerID=40&md5=f79072ae9be07fd5b9e5aef0a98753ad
Keywords: Activity Assay, Esi-Ms, Human Fibroblast Collagenase, Matrix Metalloproteinases, Biotechnology, Catalysis, Fourier Transforms, Gold, Mass Spectrometry, Surface Phenomena, Matrix Metyalloproteinase, Enzymes, Interstitial Collagenase, Matrix Metalloproteinase Inhibitor, Zinc, Cancer, Conference Paper, Electrospray Mass Spectrometry, Enzyme Activity, Enzyme Inhibitor Interaction, Extracellular Matrix, Fibrosis, Fourier Transformation, Lung Emphysema, Molecular Weight, Priority Journal, Rheumatoid Arthritis, Surface Plasmon Resonance, Catalytic Domain, Immobilized, Fourier Analysis, Hydroxamic Acids, Kinetics, Oligopeptides, Electrospray Ionization, Sulfonamides,
Affiliations:
*** IBB - CNR ***
Consorzio Interuniversitario di Ricerca in Chimica dei Metalli Nei Sistemi Biologici, Via C. Ulpiani 27, 70126, Bari, Italy
Dipartimento di Scienze Chimiche, Università di Catania, Viale Andrea Doria 6, 95125, Catania, Italy
Istituto Biostrutture e Bioimmagini, CNR, Viale A. Doria 6, Catania, Italy
Dipartimento delle Scienze Biologiche, Università degli Studi di Napoli Federico II, Via Mezzocannone 16, Napoli, Italy
Magnetic Resonance Center (CERM), University of Florence, Via L. Sacconi, 6, Sesto Fiorentino, Italy
Department of Agricultural Biotechnology, University of Florence, P.le delle Cascine, 24, Florence, Italy
References:
Not available.
J Mass Spectrom (ISSN: 1076-5174, 1096-9888), 2005 Dec; 40(12): 1565-1571.
Export to BibTeX Export to EndNote
Paper type: Journal Article,
Impact factor: 3.574, 5-year impact factor: 3.017
Url: http://www.scopus.com/inward/record.url?eid=2-s2.0-30044445496&partnerID=40&md5=f79072ae9be07fd5b9e5aef0a98753ad
Keywords: Activity Assay, Esi-Ms, Human Fibroblast Collagenase, Matrix Metalloproteinases, Biotechnology, Catalysis, Fourier Transforms, Gold, Mass Spectrometry, Surface Phenomena, Matrix Metyalloproteinase, Enzymes, Interstitial Collagenase, Matrix Metalloproteinase Inhibitor, Zinc, Cancer, Conference Paper, Electrospray Mass Spectrometry, Enzyme Activity, Enzyme Inhibitor Interaction, Extracellular Matrix, Fibrosis, Fourier Transformation, Lung Emphysema, Molecular Weight, Priority Journal, Rheumatoid Arthritis, Surface Plasmon Resonance, Catalytic Domain, Immobilized, Fourier Analysis, Hydroxamic Acids, Kinetics, Oligopeptides, Electrospray Ionization, Sulfonamides,
Affiliations:
*** IBB - CNR ***
Consorzio Interuniversitario di Ricerca in Chimica dei Metalli Nei Sistemi Biologici, Via C. Ulpiani 27, 70126, Bari, Italy
Dipartimento di Scienze Chimiche, Università di Catania, Viale Andrea Doria 6, 95125, Catania, Italy
Istituto Biostrutture e Bioimmagini, CNR, Viale A. Doria 6, Catania, Italy
Dipartimento delle Scienze Biologiche, Università degli Studi di Napoli Federico II, Via Mezzocannone 16, Napoli, Italy
Magnetic Resonance Center (CERM), University of Florence, Via L. Sacconi, 6, Sesto Fiorentino, Italy
Department of Agricultural Biotechnology, University of Florence, P.le delle Cascine, 24, Florence, Italy
References:
Not available.
Activity of anchored human matrix metalloproteinase-1 catalytic domain on Au(111) surfaces monitored by ESI-MS
Matrix metalloproteinases (MMPs) are a family of Zn-dependent endo-peptidases known for their ability to cleave several components of the extracellular matrix, but which can also cleave many non-matrix proteins. There are many evidences that MMPs are involved in physiological and pathological processes, and a huge effort has been put in the development of possible inhibitors that could reduce the activity of MMPs, as it is clear that the ability to monitor and control such activity plays a pivotal role in the search for potential drugs aimed at finding a cure for several diseases such as pulmonary emphysema, rheumatoid arthritis, fibrotic disorders and cancer. A powerful method currently available to study enzyme-inhibitor interactions is based on the use of the surface plasmon resonance (SPR) technique. When MMP interactions are studied, a procedure by which inhibitors are normally anchored on sensor chips and SPR technique is used in order to study their interaction with MMPs molecules is usually followed. This is because it is currently believed that MMPs cannot be anchored on the sensor-chip surface without losing their activity. However, this approach gives rise to problems, as the anchoring of low-molecular-weight inhibitors on gold surfaces easily affects their ability to interact with MMPs. For this reason, the anchoring of MMPs is highly desirable. A new experimental protocol that couples the Fourier transform-SPR (FT-SPR) technique with electrospray ionization-mass spectroscopy (ESI-MS) is described here for the evaluation of the activity of MMP-1 catalytic domain (cdMMP-1) anchored on gold surfaces. The cdMMP-1 surface coverage is calculated by using FT-SPR and the enzyme activity is estimated by ESI-MS. The proposed method is label-free. Copyright (c) 2005 John Wiley & Sons, Ltd.
Matrix metalloproteinases (MMPs) are a family of Zn-dependent endo-peptidases known for their ability to cleave several components of the extracellular matrix, but which can also cleave many non-matrix proteins. There are many evidences that MMPs are involved in physiological and pathological processes, and a huge effort has been put in the development of possible inhibitors that could reduce the activity of MMPs, as it is clear that the ability to monitor and control such activity plays a pivotal role in the search for potential drugs aimed at finding a cure for several diseases such as pulmonary emphysema, rheumatoid arthritis, fibrotic disorders and cancer. A powerful method currently available to study enzyme-inhibitor interactions is based on the use of the surface plasmon resonance (SPR) technique. When MMP interactions are studied, a procedure by which inhibitors are normally anchored on sensor chips and SPR technique is used in order to study their interaction with MMPs molecules is usually followed. This is because it is currently believed that MMPs cannot be anchored on the sensor-chip surface without losing their activity. However, this approach gives rise to problems, as the anchoring of low-molecular-weight inhibitors on gold surfaces easily affects their ability to interact with MMPs. For this reason, the anchoring of MMPs is highly desirable. A new experimental protocol that couples the Fourier transform-SPR (FT-SPR) technique with electrospray ionization-mass spectroscopy (ESI-MS) is described here for the evaluation of the activity of MMP-1 catalytic domain (cdMMP-1) anchored on gold surfaces. The cdMMP-1 surface coverage is calculated by using FT-SPR and the enzyme activity is estimated by ESI-MS. The proposed method is label-free. Copyright (c) 2005 John Wiley & Sons, Ltd.
Activity of anchored human matrix metalloproteinase-1 catalytic domain on Au(111) surfaces monitored by ESI-MS
| ▼ Design and screening of molecular repertoires as a source for new bioactive compounds |
Activity of anchored human matrix metalloproteinase-1 catalytic domain on Au(111) surfaces monitored by ESI-MS
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24 Records (24 excluding Abstracts).
Total impact factor: 78.692 (78.692 excluding Abstracts).
Total 5 year impact factor: 82.33 (82.33 excluding Abstracts).
Total impact factor: 78.692 (78.692 excluding Abstracts).
Total 5 year impact factor: 82.33 (82.33 excluding Abstracts).
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