LIVIVO - The Search Portal for Life Sciences

zur deutschen Oberfläche wechseln
Advanced search

Search results

Result 1 - 8 of total 8

Search options

  1. Article ; Online: A Lysosome-Targeted Tetrazine for Organelle-Specific Click-to-Release Chemistry in Antigen Presenting Cells.

    Ligthart, Nina A M / de Geus, Mark A R / van de Plassche, Merel A T / Torres García, Diana / Isendoorn, Marjolein M E / Reinalda, Luuk / Ofman, Daniëlle / van Leeuwen, Tyrza / van Kasteren, Sander I

    Journal of the American Chemical Society

    2023  Volume 145, Issue 23, Page(s) 12630–12640

    Abstract: Bioorthogonal deprotections are readily used to control biological function in a cell-specific manner. To further improve the spatial resolution of these reactions, we here present a lysosome-targeted tetrazine for an organelle-specific deprotection ... ...

    Abstract Bioorthogonal deprotections are readily used to control biological function in a cell-specific manner. To further improve the spatial resolution of these reactions, we here present a lysosome-targeted tetrazine for an organelle-specific deprotection reaction. We show that
    MeSH term(s) Click Chemistry ; Peptides ; Heterocyclic Compounds ; Organelles ; Lysosomes ; Antigen-Presenting Cells
    Chemical Substances Peptides ; Heterocyclic Compounds
    Language English
    Publishing date 2023-06-03
    Publishing country United States
    Document type Journal Article ; Research Support, Non-U.S. Gov't
    ZDB-ID 3155-0
    ISSN 1520-5126 ; 0002-7863
    ISSN (online) 1520-5126
    ISSN 0002-7863
    DOI 10.1021/jacs.3c02139
    Database MEDical Literature Analysis and Retrieval System OnLINE

    More links

    Kategorien

    In stock of ZB MED Bonn / Germany

    Z 4' 55/32: Show issues
    Z 7.3: Show issues

    Order via subito

    This service is chargeable due to the Delivery terms set by subito. Orders including an article and supplementary material will be classified as separate orders. In these cases, fees will be demanded for each order.

    Inter-library loan at ZB MED

    Your chosen title can be delivered directly to ZB MED Cologne location if you are registered as a user at ZB MED Cologne.

  2. Article ; Online: Rapid Solid-Phase Construction of Serine Hydrolase Probes Results in Selective Activity-Based Probes for Acyl Protein Thioesterases-1/2.

    Vanhoutte, Roeland / van de Plassche, Merel A T / Verhelst, Steven H L

    Journal of medicinal chemistry

    2020  Volume 63, Issue 20, Page(s) 11845–11853

    Abstract: Serine hydrolases (SHs) are a large, diverse family of enzymes that play various biomedically important roles. Their study has been substantially advanced by activity-based protein profiling, which makes use of covalent chemical probes for labeling the ... ...

    Abstract Serine hydrolases (SHs) are a large, diverse family of enzymes that play various biomedically important roles. Their study has been substantially advanced by activity-based protein profiling, which makes use of covalent chemical probes for labeling the active site and detection by various methodologies. However, highly selective probes for individual SHs are scarce because probe synthesis usually takes place by time-consuming solution phase chemistry. We here report a general solid-phase synthesis toward SH chemical probes, which will speed up probe library synthesis. It involves the construction of a recognition element ending in a secondary amine followed by capping with different electrophiles. We illustrate the power of this approach by the discovery of selective chemical probes for the depalmitoylating enzymes APT-1/2. Overall, this study reports new methodologies to synthesize SH probes, while providing new reagents to study protein depalmitoylation.
    MeSH term(s) Animals ; Cell Line, Tumor ; Dose-Response Relationship, Drug ; Enzyme Inhibitors/chemical synthesis ; Enzyme Inhibitors/chemistry ; Enzyme Inhibitors/pharmacology ; Humans ; Mice ; Models, Molecular ; Molecular Probes/chemical synthesis ; Molecular Probes/chemistry ; Molecular Probes/pharmacology ; Molecular Structure ; Solid-Phase Synthesis Techniques ; Structure-Activity Relationship ; Thiolester Hydrolases/antagonists & inhibitors ; Thiolester Hydrolases/metabolism
    Chemical Substances Enzyme Inhibitors ; Molecular Probes ; LYPLA1 protein, human (EC 3.1.2.-) ; LYPLA2 protein, human (EC 3.1.2.-) ; Thiolester Hydrolases (EC 3.1.2.-)
    Language English
    Publishing date 2020-10-13
    Publishing country United States
    Document type Journal Article ; Research Support, Non-U.S. Gov't
    ZDB-ID 218133-2
    ISSN 1520-4804 ; 0022-2623
    ISSN (online) 1520-4804
    ISSN 0022-2623
    DOI 10.1021/acs.jmedchem.0c01043
    Database MEDical Literature Analysis and Retrieval System OnLINE

    More links

    Kategorien

    In stock of ZB MED Cologne/Königswinter

    Zs.B 151: Show issues Location:
    Je nach Verfügbarkeit (siehe Angabe bei Bestand)
    bis Jg. 2021: Bestellungen von Artikeln über das Online-Bestellformular
    ab Jg. 2022: Lesesaal (EG)
    Zs.MB 1: Show issues

    Order via subito

    This service is chargeable due to the Delivery terms set by subito. Orders including an article and supplementary material will be classified as separate orders. In these cases, fees will be demanded for each order.

  3. Article: Facile Synthesis of Aminomethyl Phosphinate Esters as Serine Protease Inhibitors with Primed Site Interaction.

    Kahler, Jan Pascal / Lenders, Stijn / van de Plassche, Merel A T / Verhelst, Steven H L

    ACS medicinal chemistry letters

    2020  Volume 11, Issue 9, Page(s) 1739–1744

    Abstract: Serine proteases comprise about one-third of all proteases, and defective regulation of serine proteases is involved in numerous diseases. Therefore, serine protease inhibitors are promising drug candidates. Aminomethyl diphenyl phosphonates have been ... ...

    Abstract Serine proteases comprise about one-third of all proteases, and defective regulation of serine proteases is involved in numerous diseases. Therefore, serine protease inhibitors are promising drug candidates. Aminomethyl diphenyl phosphonates have been regularly used as scaffolds for covalent serine protease inhibition and the design of activity-based probes. However, they cannot make use of a protease's primed site. Therefore, we developed a facile two-step synthesis toward a set of phenyl phosphinates, which is a related scaffold but can interact with the primed site. We tested their inhibitory activity on five different serine proteases and found that a phenyl group directly attached to the phosphorus atom leads to superior activity compared with phosphonates.
    Language English
    Publishing date 2020-08-10
    Publishing country United States
    Document type Journal Article
    ISSN 1948-5875
    ISSN 1948-5875
    DOI 10.1021/acsmedchemlett.0c00284
    Database MEDical Literature Analysis and Retrieval System OnLINE

    More links

    Kategorien

    Order via subito

    This service is chargeable due to the Delivery terms set by subito. Orders including an article and supplementary material will be classified as separate orders. In these cases, fees will be demanded for each order.

    Inter-library loan at ZB MED

    Your chosen title can be delivered directly to ZB MED Cologne location if you are registered as a user at ZB MED Cologne.

  4. Article ; Online: Methyltetrazine as a small live-cell compatible bioorthogonal handle for imaging enzyme activities

    Torres-García, Diana / van de Plassche, Merel A T / van Boven, Emma / van Leeuwen, Tyrza / Groenewold, Mirjam G J / Sarris, Alexi J C / Klein, Luuk / Overkleeft, Herman S / van Kasteren, Sander I

    RSC chemical biology

    2022  Volume 3, Issue 11, Page(s) 1325–1330

    Abstract: Bioorthogonal chemistry combines well with activity-based protein profiling, as it allows for the introduction of detection tags without significantly influencing the physiochemical and biological functions of the probe. In this work, we introduced ... ...

    Abstract Bioorthogonal chemistry combines well with activity-based protein profiling, as it allows for the introduction of detection tags without significantly influencing the physiochemical and biological functions of the probe. In this work, we introduced methyltetrazinylalanine (MeTz-Ala), a close mimic of phenylalanine, into a dipeptide fluoromethylketone cysteine protease inhibitor. Following covalent and irreversible inhibition, the tetrazine allows vizualisation of the captured cathepsin activity by means of inverse electron demand Diels Alder ligation in cell lysates and live cells, demonstrating that tetrazines can be used as live cell compatible, minimal bioorthogonal tags in activity-based protein profiling.
    Language English
    Publishing date 2022-09-13
    Publishing country England
    Document type Journal Article
    ISSN 2633-0679
    ISSN (online) 2633-0679
    DOI 10.1039/d2cb00120a
    Database MEDical Literature Analysis and Retrieval System OnLINE

    More links

    Kategorien

    Order via subito

    This service is chargeable due to the Delivery terms set by subito. Orders including an article and supplementary material will be classified as separate orders. In these cases, fees will be demanded for each order.

    Inter-library loan at ZB MED

    Your chosen title can be delivered directly to ZB MED Cologne location if you are registered as a user at ZB MED Cologne.

  5. Article ; Online: Peptidyl Acyloxymethyl Ketones as Activity-Based Probes for the Main Protease of SARS-CoV-2*.

    van de Plassche, Merel A T / Barniol-Xicota, Marta / Verhelst, Steven H L

    Chembiochem : a European journal of chemical biology

    2020  Volume 21, Issue 23, Page(s) 3383–3388

    Abstract: The global pandemic caused by SARS-CoV-2 calls for the fast development of antiviral drugs against this particular coronavirus. Chemical tools to facilitate inhibitor discovery as well as detection of target engagement by hit or lead compounds from high- ... ...

    Abstract The global pandemic caused by SARS-CoV-2 calls for the fast development of antiviral drugs against this particular coronavirus. Chemical tools to facilitate inhibitor discovery as well as detection of target engagement by hit or lead compounds from high-throughput screens are therefore in urgent need. We here report novel, selective activity-based probes that enable detection of the SARS-CoV-2 main protease. The probes are based on acyloxymethyl ketone reactive electrophiles combined with a peptide sequence including unnatural amino acids that targets the nonprimed site of the main protease substrate binding cleft. They are the first activity-based probes for the main protease of coronaviruses and display target labeling within a human proteome without background. We expect that these reagents will be useful in the drug-development pipeline, not only for the current SARS-CoV-2, but also for other coronaviruses.
    MeSH term(s) Binding Sites ; COVID-19/diagnosis ; COVID-19/virology ; Catalytic Domain ; Coronavirus M Proteins/chemistry ; Coronavirus M Proteins/metabolism ; Humans ; Ketones/chemistry ; Ketones/metabolism ; Kinetics ; Molecular Docking Simulation ; Molecular Probes/chemistry ; Molecular Probes/metabolism ; Peptides/chemistry ; SARS-CoV-2/enzymology ; SARS-CoV-2/isolation & purification
    Chemical Substances Coronavirus M Proteins ; Ketones ; M protein, SARS-CoV ; Molecular Probes ; Peptides
    Keywords covid19
    Language English
    Publishing date 2020-09-09
    Publishing country Germany
    Document type Journal Article ; Research Support, Non-U.S. Gov't
    ZDB-ID 2020469-3
    ISSN 1439-7633 ; 1439-4227
    ISSN (online) 1439-7633
    ISSN 1439-4227
    DOI 10.1002/cbic.202000371
    Database MEDical Literature Analysis and Retrieval System OnLINE

    Full text online

    More links

    Kategorien

    Order via subito

    This service is chargeable due to the Delivery terms set by subito. Orders including an article and supplementary material will be classified as separate orders. In these cases, fees will be demanded for each order.

  6. Article ; Online: Use of Non-Natural Amino Acids for the Design and Synthesis of a Selective, Cell-Permeable MALT1 Activity-Based Probe.

    van de Plassche, Merel A T / O'Neill, Thomas J / Seeholzer, Thomas / Turk, Boris / Krappmann, Daniel / Verhelst, Steven H L

    Journal of medicinal chemistry

    2020  Volume 63, Issue 8, Page(s) 3996–4004

    Abstract: Constitutive proteolytic activity of MALT1 is associated with highly aggressive B-cell lymphomas. Chemical tools that detect active MALT1 have been reported, but suffer from poor cell permeability and/or cross-reactivity with the cysteine protease ... ...

    Abstract Constitutive proteolytic activity of MALT1 is associated with highly aggressive B-cell lymphomas. Chemical tools that detect active MALT1 have been reported, but suffer from poor cell permeability and/or cross-reactivity with the cysteine protease cathepsin B. Here, we report that the non-natural amino acid pipecolinic acid in the P2 position of substrates and chemical probes leads to improved selectivity toward MALT1 and results in cell-permeable fluorescent probes.
    MeSH term(s) Amino Acids/chemical synthesis ; Amino Acids/metabolism ; Amino Acids/pharmacology ; Cell Line, Tumor ; Cell Membrane Permeability/drug effects ; Cell Membrane Permeability/physiology ; Drug Design ; Fluorescent Dyes/chemical synthesis ; Fluorescent Dyes/metabolism ; Fluorescent Dyes/pharmacology ; Humans ; Jurkat Cells ; Mucosa-Associated Lymphoid Tissue Lymphoma Translocation 1 Protein/metabolism ; Protein Structure, Secondary ; Protein Structure, Tertiary
    Chemical Substances Amino Acids ; Fluorescent Dyes ; MALT1 protein, human (EC 3.4.22.-) ; Mucosa-Associated Lymphoid Tissue Lymphoma Translocation 1 Protein (EC 3.4.22.-)
    Language English
    Publishing date 2020-04-09
    Publishing country United States
    Document type Journal Article ; Research Support, Non-U.S. Gov't
    ZDB-ID 218133-2
    ISSN 1520-4804 ; 0022-2623
    ISSN (online) 1520-4804
    ISSN 0022-2623
    DOI 10.1021/acs.jmedchem.9b01879
    Database MEDical Literature Analysis and Retrieval System OnLINE

    More links

    Kategorien

    In stock of ZB MED Cologne/Königswinter

    Zs.B 151: Show issues Location:
    Je nach Verfügbarkeit (siehe Angabe bei Bestand)
    bis Jg. 2021: Bestellungen von Artikeln über das Online-Bestellformular
    ab Jg. 2022: Lesesaal (EG)
    Zs.MB 1: Show issues

    Order via subito

    This service is chargeable due to the Delivery terms set by subito. Orders including an article and supplementary material will be classified as separate orders. In these cases, fees will be demanded for each order.

  7. Article: Peptidyl Acyloxymethyl Ketones as Activity-Based Probes for the Main Protease of SARS-CoV-2

    van de Plassche, Merel A T / Barniol-Xicota, Marta / Verhelst, Steven H L

    Chembiochem

    Abstract: The global pandemic caused by SARS-CoV-2 calls for the fast development of antiviral drugs against this particular coronavirus. Chemical tools to facilitate inhibitor discovery as well as detection of target engagement by hit or lead compounds from high- ... ...

    Abstract The global pandemic caused by SARS-CoV-2 calls for the fast development of antiviral drugs against this particular coronavirus. Chemical tools to facilitate inhibitor discovery as well as detection of target engagement by hit or lead compounds from high-throughput screens are therefore in urgent need. We here report novel, selective activity-based probes that enable detection of the SARS-CoV-2 main protease. The probes are based on acyloxymethyl ketone reactive electrophiles combined with a peptide sequence including unnatural amino acids that targets the nonprimed site of the main protease substrate binding cleft. They are the first activity-based probes for the main protease of coronaviruses and display target labeling within a human proteome without background. We expect that these reagents will be useful in the drug-development pipeline, not only for the current SARS-CoV-2, but also for other coronaviruses.
    Keywords covid19
    Publisher WHO
    Document type Article
    Note WHO #Covidence: #676815
    Database COVID19

    Kategorien

    Inter-library loan at ZB MED

    Your chosen title can be delivered directly to ZB MED Cologne location if you are registered as a user at ZB MED Cologne.

  8. Article: Recent Advances in Activity-Based Protein Profiling of Proteases.

    Chakrabarty, Suravi / Kahler, Jan Pascal / van de Plassche, Merel A T / Vanhoutte, Roeland / Verhelst, Steven H L

    Current topics in microbiology and immunology

    2018  Volume 420, Page(s) 253–281

    Abstract: The activity of proteases is tightly regulated, and dysregulation is linked to a variety of human diseases. For this reason, ABPP is a well-suited method to study protease biology and the design of protease probes has pushed the boundaries of ABPP. The ... ...

    Abstract The activity of proteases is tightly regulated, and dysregulation is linked to a variety of human diseases. For this reason, ABPP is a well-suited method to study protease biology and the design of protease probes has pushed the boundaries of ABPP. The development of highly selective protease probes is still a challenging task. After an introduction, the first section of this chapter discusses several strategies to enable detection of a single active protease species. These range from the usage of non-natural amino acids, combination of probes with antibodies, and engineering of the target proteases. A next section describes the different types of detection tags that facilitate the read-out possibilities including various types of imaging methods and mass spectrometry-based target identification. The power of protease ABPP is illustrated by examples for a selected number of proteases. It is expected that some protease probes that have been evaluated in animal models of human disease will find translation into clinical application in the near future.
    MeSH term(s) Animals ; Endopeptidases/analysis ; Endopeptidases/chemistry ; Endopeptidases/metabolism ; Enzyme Assays/methods ; Humans ; Molecular Probe Techniques ; Peptide Hydrolases/analysis ; Peptide Hydrolases/chemistry ; Peptide Hydrolases/metabolism
    Chemical Substances Endopeptidases (EC 3.4.-) ; Peptide Hydrolases (EC 3.4.-)
    Language English
    Publishing date 2018-09-22
    Publishing country Germany
    Document type Journal Article ; Review
    ISSN 0070-217X
    ISSN 0070-217X
    DOI 10.1007/82_2018_138
    Database MEDical Literature Analysis and Retrieval System OnLINE

    Full text online

    More links

    Kategorien

    Order via subito

    This service is chargeable due to the Delivery terms set by subito. Orders including an article and supplementary material will be classified as separate orders. In these cases, fees will be demanded for each order.

    Inter-library loan at ZB MED

    Your chosen title can be delivered directly to ZB MED Cologne location if you are registered as a user at ZB MED Cologne.

To top