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Article ; Online: Cryptotanshinone from Salvia miltiorrhiza Roots Reduces Cytokeratin CK1/10 Expression in Keratinocytes by Activation of Peptidyl-prolyl-cis-trans-isomerase FKBP1A.

Esch, Stefan / König, Simone / Bopp, Bertan / Jose, Joachim / Brandt, Simone / Hensel, Andreas

2018 Volume 85, Issue 7, Page(s) 552–562

Abstract: Cryptotanshinone (CTS) (1 µM) from the roots ... ...

Abstract	Cryptotanshinone (CTS) (1 µM) from the roots of
MeSH term(s)	Cell Differentiation/drug effects ; Cell Line ; Enzyme Activation/drug effects ; Humans ; Keratinocytes/drug effects ; Keratinocytes/metabolism ; Phenanthrenes/pharmacology ; Plant Extracts/pharmacology ; Salvia miltiorrhiza/chemistry ; Tacrolimus Binding Proteins/metabolism
Chemical Substances	FKBP1A protein, human ; Phenanthrenes ; Plant Extracts ; cryptotanshinone (5E9SXT166N) ; Tacrolimus Binding Proteins (EC 5.2.1.-)
Language	English
Publishing date	2018-07-23
Publishing country	Germany
Document type	Journal Article
ZDB-ID	123545-x
ISSN	1439-0221 ; 0032-0943
ISSN (online)	1439-0221
ISSN	0032-0943
DOI	10.1055/a-0660-0441
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Article: Design and biological testing of peptidic dimerization inhibitors of human Hsp90 that target the C-terminal domain

Bopp, Bertan / Anissa Ouald-Chaib / Emanuele Ciglia / Georg Groth / Holger Gohlke / Joachim Jose

Biochimica et biophysica acta. 2016 June, v. 1860, no. 6

2016

Abstract: Small molecules targeting the dimerization interface of the C-terminal domain of Hsp90, a validated target for cancer treatment, have yet to be identified.Three peptides were designed with the aim to inhibit the dimerization of Hsp90. Computational and ... ...

Abstract	Small molecules targeting the dimerization interface of the C-terminal domain of Hsp90, a validated target for cancer treatment, have yet to be identified.Three peptides were designed with the aim to inhibit the dimerization of Hsp90. Computational and biophysical methods examined the α-helical structure for the three peptides. Based on the Autodisplay technology, a novel flow cytometer dimerization assay was developed to test inhibition of Hsp90 dimerization. Microscale thermophoresis was used to determine the KD of the peptides towards the C-terminal domain of Hsp90.MD simulations and CD spectroscopy indicated an α-helical structure for two of the three peptides. By flow cytometer analysis, IC50 values of 2.08μM for peptide H2 and 8.96μM for peptide H3 were determined. Dimer formation of the C-terminal dimerization domain was analyzed by microscale thermophoresis, and a KD of 1.29nM was determined. Furthermore, microscale thermophoresis studies demonstrated a high affinity binding of H2 and H3 to the C-terminal domain, with a KD of 1.02μM and 1.46μM, respectively.These results revealed the first peptidic inhibitors of Hsp90 dimerization targeting the C-terminal domain. Furthermore, it has been shown that these peptides bind to the C-terminal domain with a low micromolar affinity.These results can be used to design and screen for small molecules that inhibit the dimerization of the C-terminal domain of Hsp90, which could open a new route for cancer therapy.
Keywords	binding capacity ; circular dichroism spectroscopy ; dimerization ; flow cytometry ; humans ; inhibitory concentration 50 ; neoplasms ; peptides ; therapeutics
Language	English
Dates of publication	2016-06
Size	p. 1043-1055.
Publishing place	Elsevier B.V.
Document type	Article
ZDB-ID	840755-1
ISSN	0304-4165
ISSN	0304-4165
DOI	10.1016/j.bbagen.2016.01.005
Database	NAL-Catalogue (AGRICOLA)

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Article: Design and biological testing of peptidic dimerization inhibitors of human Hsp90 that target the C-terminal domain.

Bopp, Bertan / Ciglia, Emanuele / Ouald-Chaib, Anissa / Groth, Georg / Gohlke, Holger / Jose, Joachim

Biochimica et biophysica acta

2016 Volume 1860, Issue 6, Page(s) 1043–1055

Abstract: Background: Small molecules targeting the dimerization interface of the C-terminal domain of Hsp90, a validated target for cancer treatment, have yet to be identified.: Methods: Three peptides were designed with the aim to inhibit the dimerization of ...

Abstract	Background: Small molecules targeting the dimerization interface of the C-terminal domain of Hsp90, a validated target for cancer treatment, have yet to be identified. Methods: Three peptides were designed with the aim to inhibit the dimerization of Hsp90. Computational and biophysical methods examined the α-helical structure for the three peptides. Based on the Autodisplay technology, a novel flow cytometer dimerization assay was developed to test inhibition of Hsp90 dimerization. Microscale thermophoresis was used to determine the K(D) of the peptides towards the C-terminal domain of Hsp90. Results: MD simulations and CD spectroscopy indicated an α-helical structure for two of the three peptides. By flow cytometer analysis, IC(50) values of 2.08 μM for peptide H2 and 8.96 μM for peptide H3 were determined. Dimer formation of the C-terminal dimerization domain was analyzed by microscale thermophoresis, and a K(D) of 1.29 nM was determined. Furthermore, microscale thermophoresis studies demonstrated a high affinity binding of H2 and H3 to the C-terminal domain, with a K(D) of 1.02 μM and 1.46 μM, respectively. Conclusions: These results revealed the first peptidic inhibitors of Hsp90 dimerization targeting the C-terminal domain. Furthermore, it has been shown that these peptides bind to the C-terminal domain with a low micromolar affinity. General significance: These results can be used to design and screen for small molecules that inhibit the dimerization of the C-terminal domain of Hsp90, which could open a new route for cancer therapy.
MeSH term(s)	Amino Acid Sequence ; Drug Design ; HSP90 Heat-Shock Proteins/antagonists & inhibitors ; HSP90 Heat-Shock Proteins/chemistry ; HSP90 Heat-Shock Proteins/physiology ; Humans ; Molecular Dynamics Simulation ; Molecular Sequence Data ; Protein Multimerization ; Protein Structure, Secondary
Chemical Substances	HSP90 Heat-Shock Proteins
Language	English
Publishing date	2016-06
Publishing country	Netherlands
Document type	Journal Article
ZDB-ID	60-7
ISSN	1879-2596 ; 1879-260X ; 1872-8006 ; 1879-2642 ; 1879-2618 ; 1879-2650 ; 0006-3002 ; 0005-2728 ; 0005-2736 ; 0304-4165 ; 0167-4838 ; 1388-1981 ; 0167-4889 ; 0167-4781 ; 0304-419X ; 1570-9639 ; 0925-4439 ; 1874-9399
ISSN (online)	1879-2596 ; 1879-260X ; 1872-8006 ; 1879-2642 ; 1879-2618 ; 1879-2650
ISSN	0006-3002 ; 0005-2728 ; 0005-2736 ; 0304-4165 ; 0167-4838 ; 1388-1981 ; 0167-4889 ; 0167-4781 ; 0304-419X ; 1570-9639 ; 0925-4439 ; 1874-9399
DOI	10.1016/j.bbagen.2016.01.005
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Article: Cryptotanshinone from Salvia miltiorrhiza Roots Reduces Cytokeratin CK1/10 Expression in Keratinocytes by Activation of Peptidyl-prolyl-cis-trans-isomerase FKBP1A

Esch, Stefan / König, Simone / Bopp, Bertan / Jose, Joachim / Brandt, Simone / Hensel, Andreas

Planta Medica

2018 Volume 85, Issue 07, Page(s) 552–562

Abstract: Cryptotanshinone (CTS) (1 µM) from the roots of Salvia miltiorrhiza exerts a strong influence on the terminal differentiation of human keratinocytes (HaCaT cell line, primary natural human keratinocytes) and downregulates the expression of ... ...

Abstract	Cryptotanshinone (CTS) (1 µM) from the roots of Salvia miltiorrhiza exerts a strong influence on the terminal differentiation of human keratinocytes (HaCaT cell line, primary natural human keratinocytes) and downregulates the expression of differentiation-specific cytokeratins CK1 and CK10 on protein and gene level. Other differentiation specific proteins as involucrin, filaggrin, loricrin, and transglutaminase were not affected to a higher extent. CTS (1 µM) did not influence the cell viability and the proliferation of keratinocytes. Using a combination of drug affinity response target stability assay in combination with a proteomic approach and multivariate statistics for target elucidation, peptidyl-prolyl-cis-trans-isomerase FKBP1A (known target of inhibitors such as tacrolimus or rapamycin) was addressed as potential molecular target of CTS. The interaction of CTS with FKBP1A was additionally shown by thermal shift and enzymatic activity assays. Interestingly, CTS served as an activator of FKBP1A, which led to a reduced activity of the TGF β receptor pathway and therefore to a diminished CK1 and CK10 expression. The combination of the FKBP1A activator CTS with the inhibitor tacrolimus neutralized the effects of both compounds. From these data, a potential dermatological use of CTS and CTS-containing plant extracts (e.g., hydroalcoholic extract from the roots of S. miltiorrhiza ) for keratinopathic ichthyosis, a disease characterized by overexpression of CK1 and CK10, is discussed. This study displays an experimental strategy for combining phytochemical aspects on active natural products with systematic identification of molecular targets on gene, protein, and cell level.
Keywords	CFKBP1A ; cryptotanshinone ; differentiation ; keratinocytes ; Lamiaceae ; TGF ; receptor
Language	English
Publishing date	2018-07-23
Publisher	Georg Thieme Verlag KG
Publishing place	Stuttgart ; New York
Document type	Article
ZDB-ID	123545-x
ISSN	1439-0221 ; 0032-0943
ISSN (online)	1439-0221
ISSN	0032-0943
DOI	10.1055/a-0660-0441
Database	Thieme publisher's database

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Article: Development of a First-in-Class Small-Molecule Inhibitor of the C-Terminal Hsp90 Dimerization.

Bhatia, Sanil / Spanier, Lukas / Bickel, David / Dienstbier, Niklas / Woloschin, Vitalij / Vogt, Melina / Pols, Henrik / Lungerich, Beate / Reiners, Jens / Aghaallaei, Narges / Diedrich, Daniela / Frieg, Benedikt / Schliehe-Diecks, Julian / Bopp, Bertan / Lang, Franziska / Gopalswamy, Mohanraj / Loschwitz, Jennifer / Bajohgli, Baubak / Skokowa, Julia /

Borkhardt, Arndt / Hauer, Julia / Hansen, Finn K / Smits, Sander H J / Jose, Joachim / Gohlke, Holger / Kurz, Thomas

ACS central science

2022 Volume 8, Issue 5, Page(s) 636–655

Abstract: Heat shock proteins 90 (Hsp90) are promising therapeutic targets due to their involvement in stabilizing several aberrantly expressed oncoproteins. In cancerous cells, Hsp90 expression is elevated, thereby exerting antiapoptotic effects, which is ... ...

Abstract	Heat shock proteins 90 (Hsp90) are promising therapeutic targets due to their involvement in stabilizing several aberrantly expressed oncoproteins. In cancerous cells, Hsp90 expression is elevated, thereby exerting antiapoptotic effects, which is essential for the malignant transformation and tumor progression. Most of the Hsp90 inhibitors (Hsp90i) under investigation target the ATP binding site in the N-terminal domain of Hsp90. However, adverse effects, including induction of the prosurvival resistance mechanism (heat shock response or HSR) and associated dose-limiting toxicity, have so far precluded their clinical approval. In contrast, modulators that interfere with the C-terminal domain (CTD) of Hsp90 do not inflict HSR. Since the CTD dimerization of Hsp90 is essential for its chaperone activity, interfering with the dimerization process by small-molecule protein-protein interaction inhibitors is a promising strategy for anticancer drug research. We have developed a first-in-class small-molecule inhibitor (
Language	English
Publishing date	2022-04-27
Publishing country	United States
Document type	Journal Article
ISSN	2374-7943
ISSN	2374-7943
DOI	10.1021/acscentsci.2c00013
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Article ; Online: Naphthol AS-E Phosphate Inhibits the Activity of the Transcription Factor Myb by Blocking the Interaction with the KIX Domain of the Coactivator p300.

Uttarkar, Sagar / Dukare, Sandeep / Bopp, Bertan / Goblirsch, Michael / Jose, Joachim / Klempnauer, Karl-Heinz

Molecular cancer therapeutics

2015 Volume 14, Issue 6, Page(s) 1276–1285

Abstract: The transcription factor c-Myb is highly expressed in hematopoietic progenitor cells and controls the transcription of genes important for lineage determination, cell proliferation, and differentiation. Deregulation of c-Myb has been implicated in the ... ...

Abstract	The transcription factor c-Myb is highly expressed in hematopoietic progenitor cells and controls the transcription of genes important for lineage determination, cell proliferation, and differentiation. Deregulation of c-Myb has been implicated in the development of leukemia and certain other types of human cancer. c-Myb activity is highly dependent on the interaction of the c-Myb with the KIX domain of the coactivator p300, making the disruption of this interaction a reasonable strategy for the development of Myb inhibitors. Here, we have used bacterial Autodisplay to develop an in vitro binding assay that mimics the interaction of Myb and the KIX domain of p300. We have used this binding assay to investigate the potential of Naphthol AS-E phosphate, a compound known to bind to the KIX domain, to disrupt the interaction between Myb and p300. Our data show that Naphthol AS-E phosphate interferes with the Myb-KIX interaction in vitro and inhibits Myb activity in vivo. By using several human leukemia cell lines, we demonstrate that Naphthol AS-E phosphate suppresses the expression of Myb target genes and induces myeloid differentiation and apoptosis. Our work identifies Naphthol AS-E phosphate as the first low molecular weight compound that inhibits Myb activity by disrupting its interaction with p300, and suggests that inhibition of the Myb-KIX interaction might be a useful strategy for the treatment of leukemia and other tumors caused by deregulated c-Myb.
MeSH term(s)	Apoptosis/drug effects ; Apoptosis/genetics ; Binding Sites/genetics ; Blotting, Western ; Cell Differentiation/drug effects ; Cell Differentiation/genetics ; Cell Line, Tumor ; E1A-Associated p300 Protein/genetics ; E1A-Associated p300 Protein/metabolism ; Gene Expression Regulation, Leukemic/genetics ; HL-60 Cells ; Humans ; Microscopy, Fluorescence ; Naphthols/metabolism ; Naphthols/pharmacology ; Organophosphates/metabolism ; Organophosphates/pharmacology ; Protein Binding/drug effects ; Proto-Oncogene Proteins c-myb/antagonists & inhibitors ; Proto-Oncogene Proteins c-myb/genetics ; Proto-Oncogene Proteins c-myb/metabolism ; Reverse Transcriptase Polymerase Chain Reaction ; U937 Cells
Chemical Substances	Naphthols ; Organophosphates ; Proto-Oncogene Proteins c-myb ; naphthol AS-E phosphate ; E1A-Associated p300 Protein (EC 2.3.1.48) ; EP300 protein, human (EC 2.3.1.48)
Language	English
Publishing date	2015-03-04
Publishing country	United States
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	2063563-1
ISSN	1538-8514 ; 1535-7163
ISSN (online)	1538-8514
ISSN	1535-7163
DOI	10.1158/1535-7163.MCT-14-0662
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Article ; Online: First structure of protein kinase CK2 catalytic subunit with an effective CK2β-competitive ligand.

Raaf, Jennifer / Guerra, Barbara / Neundorf, Ines / Bopp, Bertan / Issinger, Olaf-Georg / Jose, Joachim / Pietsch, Markus / Niefind, Karsten

ACS chemical biology

2013 Volume 8, Issue 5, Page(s) 901–907

Abstract: The constitutively active Ser/Thr kinase CK2 (casein kinase 2) is used by tumor cells to acquire apoptosis resistance. CK2 exists as a heterotetrameric holoenzyme with two catalytic chains (CK2α) attached to a dimer of noncatalytic subunits (CK2β). A ... ...

Abstract	The constitutively active Ser/Thr kinase CK2 (casein kinase 2) is used by tumor cells to acquire apoptosis resistance. CK2 exists as a heterotetrameric holoenzyme with two catalytic chains (CK2α) attached to a dimer of noncatalytic subunits (CK2β). A druggable cavity at the CK2β interface of CK2α allows the design of small molecules disturbing the CK2α/CK2β interaction and thus affecting activity, stability, and substrate specificity. We describe here the first structure of CK2α with an effective CK2β-competitive compound, namely, a 13-meric cyclic peptide derived from the C-terminal CK2β segment. Some well-ordered water molecules not visible in CK2 holoenzyme structures were detected at the interface. Driven mainly by enthalpy, the peptide binds with submicromolar affinity to CK2α, stimulates its catalytic activity, and reduces effectively the CK2α/CK2β affinity. The results provide a thermodynamic and structural rationalization of the peptide's CK2β-competitive functionality and pave thus the way to a peptidomimetic drug addressing the CK2α/CK2β interaction.
MeSH term(s)	Alanine/chemistry ; Amino Acid Substitution ; Binding, Competitive ; Calorimetry/methods ; Casein Kinase II/chemistry ; Casein Kinase II/genetics ; Casein Kinase II/metabolism ; Catalytic Domain ; Crystallography, X-Ray ; Ligands ; Peptide Fragments/chemistry ; Peptide Fragments/metabolism ; Peptides, Cyclic/metabolism ; Protein Conformation ; Thermodynamics ; Tyrosine/chemistry
Chemical Substances	Ligands ; Peptide Fragments ; Peptides, Cyclic ; Tyrosine (42HK56048U) ; CSNK2A1 protein, human (EC 2.7.11.1) ; Casein Kinase II (EC 2.7.11.1) ; Alanine (OF5P57N2ZX)
Language	English
Publishing date	2013-03-18
Publishing country	United States
Document type	Letter ; Research Support, Non-U.S. Gov't
ISSN	1554-8937
ISSN (online)	1554-8937
DOI	10.1021/cb3007133
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Article ; Online: Targeting HSP90 dimerization via the C terminus is effective in imatinib-resistant CML and lacks the heat shock response.

Bhatia, Sanil / Diedrich, Daniela / Frieg, Benedikt / Ahlert, Heinz / Stein, Stefan / Bopp, Bertan / Lang, Franziska / Zang, Tao / Kröger, Tobias / Ernst, Thomas / Kögler, Gesine / Krieg, Andreas / Lüdeke, Steffen / Kunkel, Hana / Rodrigues Moita, Ana J / Kassack, Matthias U / Marquardt, Viktoria / Opitz, Friederike V / Oldenburg, Marina /

Remke, Marc / Babor, Florian / Grez, Manuel / Hochhaus, Andreas / Borkhardt, Arndt / Groth, Georg / Nagel-Steger, Luitgard / Jose, Joachim / Kurz, Thomas / Gohlke, Holger / Hansen, Finn K / Hauer, Julia

Blood

2018 Volume 132, Issue 3, Page(s) 307–320

Abstract: Heat shock protein 90 (HSP90) stabilizes many client proteins, including the BCR-ABL1 oncoprotein. BCR-ABL1 is the hallmark of chronic myeloid leukemia (CML) in which treatment-free remission (TFR) is limited, with clinical and economic consequences. ... ...

Abstract	Heat shock protein 90 (HSP90) stabilizes many client proteins, including the BCR-ABL1 oncoprotein. BCR-ABL1 is the hallmark of chronic myeloid leukemia (CML) in which treatment-free remission (TFR) is limited, with clinical and economic consequences. Thus, there is an urgent need for novel therapeutics that synergize with current treatment approaches. Several inhibitors targeting the N-terminal domain of HSP90 are under investigation, but side effects such as induction of the heat shock response (HSR) and toxicity have so far precluded their US Food and Drug Administration approval. We have developed a novel inhibitor (aminoxyrone [AX]) of HSP90 function by targeting HSP90 dimerization via the C-terminal domain. This was achieved by structure-based molecular design, chemical synthesis, and functional preclinical in vitro and in vivo validation using CML cell lines and patient-derived CML cells. AX is a promising potential candidate that induces apoptosis in the leukemic stem cell fraction (CD34
MeSH term(s)	Animals ; Antineoplastic Agents/chemistry ; Antineoplastic Agents/pharmacology ; Binding Sites ; Biomarkers, Tumor ; Cell Cycle/drug effects ; Cell Line, Tumor ; Cell Survival/drug effects ; Disease Models, Animal ; Drug Resistance, Neoplasm/drug effects ; Fusion Proteins, bcr-abl/antagonists & inhibitors ; Fusion Proteins, bcr-abl/chemistry ; HSP90 Heat-Shock Proteins/antagonists & inhibitors ; HSP90 Heat-Shock Proteins/chemistry ; HSP90 Heat-Shock Proteins/metabolism ; Heat-Shock Response/drug effects ; Humans ; Imatinib Mesylate/chemistry ; Imatinib Mesylate/pharmacology ; Leukemia, Myelogenous, Chronic, BCR-ABL Positive/drug therapy ; Leukemia, Myelogenous, Chronic, BCR-ABL Positive/metabolism ; Mice ; Models, Molecular ; Molecular Conformation ; Molecular Structure ; Protein Binding ; Protein Interaction Domains and Motifs ; Protein Kinase Inhibitors/chemistry ; Protein Kinase Inhibitors/pharmacology ; Protein Multimerization/drug effects ; Spectrum Analysis ; Structure-Activity Relationship ; Xenograft Model Antitumor Assays
Chemical Substances	Antineoplastic Agents ; Biomarkers, Tumor ; HSP90 Heat-Shock Proteins ; Protein Kinase Inhibitors ; Imatinib Mesylate (8A1O1M485B) ; Fusion Proteins, bcr-abl (EC 2.7.10.2)
Language	English
Publishing date	2018-05-03
Publishing country	United States
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	80069-7
ISSN	1528-0020 ; 0006-4971
ISSN (online)	1528-0020
ISSN	0006-4971
DOI	10.1182/blood-2017-10-810986
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Article: Design and biological testing of peptidic dimerization inhibitors of human Hsp90 that target the C-terminal domain

Bopp, Bertan / Emanuele CigliaauthorInstitute for Pharmaceutical and Medicinal Chemistry, Heinrich Heine University DÃ¼sseldorf, DÃ¼sseldorf, Germany / Anissa Ouald-ChaibauthorInstitute for Pharmaceutical and Medicinal Chemistry, Heinrich Heine University DÃ¼sseldorf, DÃ¼sseldorf, Germany / Georg GrothauthorInstitute for Biochemical Plant Physiology, Heinrich Heine University DÃ¼sseldorf, DÃ¼sseldorf, Germany / Holger GohlkeauthorInstitute for Pharmaceutical and Medicinal Chemistry, Heinrich Heine University DÃ¼sseldorf, DÃ¼sseldorf, Germany / Joachim JoseauthorInstitute for Pharmaceutical and Medicinal Chemistry, PharmaCampus, Westphalian Wilhelms-University, MÃ¼nster, Germany

Language	English
Document type	Article
Database	AGRIS - International Information System for the Agricultural Sciences and Technology

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