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An Activity-Based Probe for Cathepsin K Imaging with Excellent Potency and Selectivity
C. Lemke, J. Benýšek, D. Brajtenbach, C. Breuer, A. Jílková, M. Horn, M. Buša, L. Ulrychová, A. Illies, KF. Kubatzky, U. Bartz, M. Mareš, M. Gütschow
Journal of medicinal chemistry.
2021 ;
64 (18) :
13793-13806.
[pub] 20210902
Jazyk angličtina Země Spojené státy americké
Typ dokumentu časopisecké články, práce podpořená grantem
Perzistentní odkaz
https://www.medvik.cz/link/bmc22003678
- MeSH
- akrylamidy chemická syntéza chemie metabolismus MeSH
- fluorescenční barviva chemická syntéza chemie metabolismus MeSH
- fluorescenční mikroskopie MeSH
- inhibitory cysteinových proteinas chemická syntéza chemie metabolismus MeSH
- katalytická doména MeSH
- kathepsin K antagonisté a inhibitory chemie metabolismus MeSH
- konfokální mikroskopie MeSH
- lidé MeSH
- nádorové buněčné linie MeSH
- racionální návrh léčiv MeSH
- vazba proteinů MeSH
- Check Tag
- lidé MeSH
- Publikační typ
- časopisecké články MeSH
- práce podpořená grantem MeSH
The cysteine protease cathepsin K is a target for the treatment of diseases associated with high bone turnover. Cathepsin K is mainly expressed in osteoclasts and responsible for the destruction of the proteinaceous components of the bone matrix. We designed various fluorescent activity-based probes (ABPs) and their precursors that bind to and inactivate cathepsin K. ABP 25 exhibited extraordinary potency (kinac/Ki = 35,300 M-1s-1) and selectivity for human cathepsin K. Crystal structures of cathepsin K in complex with ABP 25 and its nonfluorescent precursor 21 were determined to characterize the binding mode of this new type of acrylamide-based Michael acceptor with the particular orientation of the dibenzylamine moiety to the primed subsite region. The cyanine-5 containing probe 25 allowed for sensitive detection of cathepsin K, selective visualization in complex proteomes, and live cell imaging of a human osteosarcoma cell line, underlining its applicability in a pathophysiological environment.
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- $a 10.1021/acs.jmedchem.1c01178 $2 doi
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- $a Lemke, Carina $u Pharmaceutical Institute, Pharmaceutical & Medicinal Chemistry, University of Bonn, An der Immenburg 4, Bonn 53121, Germany
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- $a An Activity-Based Probe for Cathepsin K Imaging with Excellent Potency and Selectivity / $c C. Lemke, J. Benýšek, D. Brajtenbach, C. Breuer, A. Jílková, M. Horn, M. Buša, L. Ulrychová, A. Illies, KF. Kubatzky, U. Bartz, M. Mareš, M. Gütschow
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- $a The cysteine protease cathepsin K is a target for the treatment of diseases associated with high bone turnover. Cathepsin K is mainly expressed in osteoclasts and responsible for the destruction of the proteinaceous components of the bone matrix. We designed various fluorescent activity-based probes (ABPs) and their precursors that bind to and inactivate cathepsin K. ABP 25 exhibited extraordinary potency (kinac/Ki = 35,300 M-1s-1) and selectivity for human cathepsin K. Crystal structures of cathepsin K in complex with ABP 25 and its nonfluorescent precursor 21 were determined to characterize the binding mode of this new type of acrylamide-based Michael acceptor with the particular orientation of the dibenzylamine moiety to the primed subsite region. The cyanine-5 containing probe 25 allowed for sensitive detection of cathepsin K, selective visualization in complex proteomes, and live cell imaging of a human osteosarcoma cell line, underlining its applicability in a pathophysiological environment.
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- $a Benýšek, Jakub $u Institute of Organic Chemistry and Biochemistry of the Czech Academy of Sciences, Flemingovo n. 2, Prague 16610, Czech Republic $u First Faculty of Medicine, Charles University, Kateřinská 32, Prague 12108, Czech Republic
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- $a Brajtenbach, Dominik $u Pharmaceutical Institute, Pharmaceutical & Medicinal Chemistry, University of Bonn, An der Immenburg 4, Bonn 53121, Germany
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- $a Breuer, Christian $u Pharmaceutical Institute, Pharmaceutical & Medicinal Chemistry, University of Bonn, An der Immenburg 4, Bonn 53121, Germany $u Department of Natural Sciences, University of Applied Sciences Bonn-Rhein-Sieg, von-Liebig-Str. 20, Rheinbach 53359, Germany
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- $a Jílková, Adéla $u Institute of Organic Chemistry and Biochemistry of the Czech Academy of Sciences, Flemingovo n. 2, Prague 16610, Czech Republic
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- $a Buša, Michal $u Institute of Organic Chemistry and Biochemistry of the Czech Academy of Sciences, Flemingovo n. 2, Prague 16610, Czech Republic $u Department of Biochemistry, Faculty of Science, Charles University, Hlavova 8, Prague 12800, Czech Republic $7 xx0321915
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- $a Ulrychová, Lenka $u Institute of Organic Chemistry and Biochemistry of the Czech Academy of Sciences, Flemingovo n. 2, Prague 16610, Czech Republic
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- $a Illies, Annika $u Pharmaceutical Institute, Pharmaceutical & Medicinal Chemistry, University of Bonn, An der Immenburg 4, Bonn 53121, Germany
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- $a Kubatzky, Katharina F $u Department of Infectious Diseases, Medical Microbiology and Hygiene, Heidelberg University Hospital, Im Neuenheimer Feld 324, Heidelberg 69120, Germany
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- $a Bartz, Ulrike $u Department of Natural Sciences, University of Applied Sciences Bonn-Rhein-Sieg, von-Liebig-Str. 20, Rheinbach 53359, Germany
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- $a Mareš, Michael $u Institute of Organic Chemistry and Biochemistry of the Czech Academy of Sciences, Flemingovo n. 2, Prague 16610, Czech Republic
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- $a Gütschow, Michael $u Pharmaceutical Institute, Pharmaceutical & Medicinal Chemistry, University of Bonn, An der Immenburg 4, Bonn 53121, Germany
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