Aminobenzothiazole derivatives stabilize the thermolabile p53 cancer mutant Y220C and show anticancer activity in p53-Y220C cell lines

Many cancers have the tumor suppressor p53 inactivated by mutation, making reactivation of mutant p53 with small molecules a promising strategy for the development of novel anticancer therapeutics. The oncogenic p53 mutation Y220C, which accounts for approximately 100,000 cancer cases per year, crea...

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Vydáno v:European journal of medicinal chemistry Ročník 152; s. 101 - 114
Hlavní autoři: Baud, Matthias G.J., Bauer, Matthias R., Verduci, Lorena, Dingler, Felix A., Patel, Ketan J., Horil Roy, Deeptee, Joerger, Andreas C., Fersht, Alan R.
Médium: Journal Article
Jazyk:angličtina
Vydáno: ISSY-LES-MOULINEAUX Elsevier Masson SAS 25.05.2018
Elsevier
Editions Scientifiques Elsevier
Témata:
Anticancer therapy
Antineoplastic Agents - chemical synthesis
Antineoplastic Agents - chemistry
Antineoplastic Agents - pharmacology
Benzothiazoles - chemical synthesis
Benzothiazoles - chemistry
Benzothiazoles - pharmacology
Cell Proliferation - drug effects
Cell Survival - drug effects
Chemistry, Medicinal
Dose-Response Relationship, Drug
Drug Screening Assays, Antitumor
Humans
Life Sciences & Biomedicine
Molecular Structure
Mutant p53
Pharmacology & Pharmacy
Real-Time Polymerase Chain Reaction
Science & Technology
Signal Transduction - drug effects
Signal Transduction - genetics
Structure-Activity Relationship
Structure-based drug discovery
Tumor Cells, Cultured
Tumor Suppressor Protein p53 - genetics
Tumor Suppressor Protein p53 - metabolism
Anticancer therapy
Structure-based drug discovery
Mutant p53
WILD-TYPE
DNA-BINDING
DESIGN
PROTEIN
TP53 MUTATION
GLIDE
CORE DOMAIN
RESCUE
ACCURATE DOCKING
REACTIVATION
ISSN:0223-5234, 1768-3254, 1768-3254
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Abstract Many cancers have the tumor suppressor p53 inactivated by mutation, making reactivation of mutant p53 with small molecules a promising strategy for the development of novel anticancer therapeutics. The oncogenic p53 mutation Y220C, which accounts for approximately 100,000 cancer cases per year, creates an extended surface crevice in the DNA-binding domain, which destabilizes p53 and causes denaturation and aggregation. Here, we describe the structure-guided design of a novel class of small-molecule Y220C stabilizers and the challenging synthetic routes developed in the process. The synthesized chemical probe MB710, an aminobenzothiazole derivative, binds tightly to the Y220C pocket and stabilizes p53-Y220C in vitro. MB725, an ethylamide analogue of MB710, induced selective viability reduction in several p53-Y220C cancer cell lines while being well tolerated in control cell lines. Reduction of viability correlated with increased and selective transcription of p53 target genes such as BTG2, p21, PUMA, FAS, TNF, and TNFRSF10B, which promote apoptosis and cell cycle arrest, suggesting compound-mediated transcriptional activation of the Y220C mutant. Our data provide a framework for the development of a class of potent, non-toxic compounds for reactivating the Y220C mutant in anticancer therapy. [Display omitted] •Proof-of-concept molecules stabilize the oncogenic protein p53-Y220C in vitro.•Molecule MB725 shows selective anticancer activity in p53-Y220C cancer cells.•Anticancer activity correlates with enhancement of p53 signaling by MB725.
AbstractList Many cancers have the tumor suppressor p53 inactivated by mutation, making reactivation of mutant p53 with small molecules a promising strategy for the development of novel anticancer therapeutics. The oncogenic p53 mutation Y220C, which accounts for approximately 100,000 cancer cases per year, creates an extended surface crevice in the DNA-binding domain, which destabilizes p53 and causes denaturation and aggregation. Here, we describe the structure-guided design of a novel class of small-molecule Y220C stabilizers and the challenging synthetic routes developed in the process. The synthesized chemical probe MB710, an aminobenzothiazole derivative, binds tightly to the Y220C pocket and stabilizes p53-Y220C in vitro. MB725, an ethylamide analogue of MB710, induced selective viability reduction in several p53-Y220C cancer cell lines while being well tolerated in control cell lines. Reduction of viability correlated with increased and selective transcription of p53 target genes such as BTG2, p21, PUMA, FAS, TNF, and TNFRSF10B, which promote apoptosis and cell cycle arrest, suggesting compound-mediated transcriptional activation of the Y220C mutant. Our data provide a framework for the development of a class of potent, non-toxic compounds for reactivating the Y220C mutant in anticancer therapy. [Display omitted] •Proof-of-concept molecules stabilize the oncogenic protein p53-Y220C in vitro.•Molecule MB725 shows selective anticancer activity in p53-Y220C cancer cells.•Anticancer activity correlates with enhancement of p53 signaling by MB725.
Many cancers have the tumor suppressor p53 inactivated by mutation, making reactivation of mutant p53 with small molecules a promising strategy for the development of novel anticancer therapeutics. The oncogenic p53 mutation Y220C, which accounts for approximately 100,000 cancer cases per year, creates an extended surface crevice in the DNA-binding domain, which destabilizes p53 and causes denaturation and aggregation. Here, we describe the structure-guided design of a novel class of small-molecule Y220C stabilizers and the challenging synthetic routes developed in the process. The synthesized chemical probe MB710, an aminobenzothiazole derivative, binds tightly to the Y220C pocket and stabilizes p53-Y220C in vitro. MB725, an ethylamide analogue of MB710, induced selective viability reduction in several p53-Y220C cancer cell lines while being well tolerated in control cell lines. Reduction of viability correlated with increased and selective transcription of p53 target genes such as BTG2, p21, PUMA, FAS, TNF, and TNFRSFIOB, which promote apoptosis and cell cycle arrest, suggesting compound-mediated transcriptional activation of the Y220C mutant. Our data provide a framework for the development of a class of potent, non-toxic compounds for reactivating the Y220C mutant in anticancer therapy. (C) 2018 MRC Laboratory of Molecular Biology. Published by Elsevier Masson SAS.
Many cancers have the tumor suppressor p53 inactivated by mutation, making reactivation of mutant p53 with small molecules a promising strategy for the development of novel anticancer therapeutics. The oncogenic p53 mutation Y220C, which accounts for approximately 100,000 cancer cases per year, creates an extended surface crevice in the DNA-binding domain, which destabilizes p53 and causes denaturation and aggregation. Here, we describe the structure-guided design of a novel class of small-molecule Y220C stabilizers and the challenging synthetic routes developed in the process. The synthesized chemical probe MB710, an aminobenzothiazole derivative, binds tightly to the Y220C pocket and stabilizes p53-Y220C in vitro. MB725, an ethylamide analogue of MB710, induced selective viability reduction in several p53-Y220C cancer cell lines while being well tolerated in control cell lines. Reduction of viability correlated with increased and selective transcription of p53 target genes such as BTG2, p21, PUMA, FAS, TNF, and TNFRSF10B, which promote apoptosis and cell cycle arrest, suggesting compound-mediated transcriptional activation of the Y220C mutant. Our data provide a framework for the development of a class of potent, non-toxic compounds for reactivating the Y220C mutant in anticancer therapy. Image 1 • Proof-of-concept molecules stabilize the oncogenic protein p53-Y220C in vitro. • Molecule MB725 shows selective anticancer activity in p53-Y220C cancer cells. • Anticancer activity correlates with enhancement of p53 signaling by MB725.
Many cancers have the tumor suppressor p53 inactivated by mutation, making reactivation of mutant p53 with small molecules a promising strategy for the development of novel anticancer therapeutics. The oncogenic p53 mutation Y220C, which accounts for approximately 100,000 cancer cases per year, creates an extended surface crevice in the DNA-binding domain, which destabilizes p53 and causes denaturation and aggregation. Here, we describe the structure-guided design of a novel class of small-molecule Y220C stabilizers and the challenging synthetic routes developed in the process. The synthesized chemical probe MB710, an aminobenzothiazole derivative, binds tightly to the Y220C pocket and stabilizes p53-Y220C in vitro. MB725, an ethylamide analogue of MB710, induced selective viability reduction in several p53-Y220C cancer cell lines while being well tolerated in control cell lines. Reduction of viability correlated with increased and selective transcription of p53 target genes such as BTG2, p21, PUMA, FAS, TNF, and TNFRSF10B, which promote apoptosis and cell cycle arrest, suggesting compound-mediated transcriptional activation of the Y220C mutant. Our data provide a framework for the development of a class of potent, non-toxic compounds for reactivating the Y220C mutant in anticancer therapy.Many cancers have the tumor suppressor p53 inactivated by mutation, making reactivation of mutant p53 with small molecules a promising strategy for the development of novel anticancer therapeutics. The oncogenic p53 mutation Y220C, which accounts for approximately 100,000 cancer cases per year, creates an extended surface crevice in the DNA-binding domain, which destabilizes p53 and causes denaturation and aggregation. Here, we describe the structure-guided design of a novel class of small-molecule Y220C stabilizers and the challenging synthetic routes developed in the process. The synthesized chemical probe MB710, an aminobenzothiazole derivative, binds tightly to the Y220C pocket and stabilizes p53-Y220C in vitro. MB725, an ethylamide analogue of MB710, induced selective viability reduction in several p53-Y220C cancer cell lines while being well tolerated in control cell lines. Reduction of viability correlated with increased and selective transcription of p53 target genes such as BTG2, p21, PUMA, FAS, TNF, and TNFRSF10B, which promote apoptosis and cell cycle arrest, suggesting compound-mediated transcriptional activation of the Y220C mutant. Our data provide a framework for the development of a class of potent, non-toxic compounds for reactivating the Y220C mutant in anticancer therapy.
Many cancers have the tumor suppressor p53 inactivated by mutation, making reactivation of mutant p53 with small molecules a promising strategy for the development of novel anticancer therapeutics. The oncogenic p53 mutation Y220C, which accounts for approximately 100,000 cancer cases per year, creates an extended surface crevice in the DNA-binding domain, which destabilizes p53 and causes denaturation and aggregation. Here, we describe the structure-guided design of a novel class of small-molecule Y220C stabilizers and the challenging synthetic routes developed in the process. The synthesized chemical probe MB710, an aminobenzothiazole derivative, binds tightly to the Y220C pocket and stabilizes p53-Y220C in vitro. MB725, an ethylamide analogue of MB710, induced selective viability reduction in several p53-Y220C cancer cell lines while being well tolerated in control cell lines. Reduction of viability correlated with increased and selective transcription of p53 target genes such as BTG2, p21, PUMA, FAS, TNF, and TNFRSF10B, which promote apoptosis and cell cycle arrest, suggesting compound-mediated transcriptional activation of the Y220C mutant. Our data provide a framework for the development of a class of potent, non-toxic compounds for reactivating the Y220C mutant in anticancer therapy.
Author Horil Roy, Deeptee
Baud, Matthias G.J.
Bauer, Matthias R.
Verduci, Lorena
Dingler, Felix A.
Patel, Ketan J.
Joerger, Andreas C.
Fersht, Alan R.
AuthorAffiliation c German Cancer Consortium (DKTK), German Cancer Center (DKFZ), 69120 Heidelberg, Institute of Pharmaceutical Chemistry, Johann Wolfgang Goethe University, Max-von-Laue-Str. 9, Frankfurt am Main, 60438, Germany
b Chemistry, Faculty of Natural and Environmental Sciences, University of Southampton, Southampton, SO17 1BJ, UK
a Medical Research Council, Laboratory of Molecular Biology, Francis Crick Avenue, Cambridge, CB2 0QH, United Kingdom
AuthorAffiliation_xml – name: a Medical Research Council, Laboratory of Molecular Biology, Francis Crick Avenue, Cambridge, CB2 0QH, United Kingdom
– name: c German Cancer Consortium (DKTK), German Cancer Center (DKFZ), 69120 Heidelberg, Institute of Pharmaceutical Chemistry, Johann Wolfgang Goethe University, Max-von-Laue-Str. 9, Frankfurt am Main, 60438, Germany
– name: b Chemistry, Faculty of Natural and Environmental Sciences, University of Southampton, Southampton, SO17 1BJ, UK
Author_xml – sequence: 1
  givenname: Matthias G.J.
  orcidid: 0000-0003-3714-4350
  surname: Baud
  fullname: Baud, Matthias G.J.
  email: m.baud@soton.ac.uk
  organization: Medical Research Council, Laboratory of Molecular Biology, Francis Crick Avenue, Cambridge, CB2 0QH, United Kingdom
– sequence: 2
  givenname: Matthias R.
  surname: Bauer
  fullname: Bauer, Matthias R.
  organization: Medical Research Council, Laboratory of Molecular Biology, Francis Crick Avenue, Cambridge, CB2 0QH, United Kingdom
– sequence: 3
  givenname: Lorena
  surname: Verduci
  fullname: Verduci, Lorena
  organization: Medical Research Council, Laboratory of Molecular Biology, Francis Crick Avenue, Cambridge, CB2 0QH, United Kingdom
– sequence: 4
  givenname: Felix A.
  surname: Dingler
  fullname: Dingler, Felix A.
  organization: Medical Research Council, Laboratory of Molecular Biology, Francis Crick Avenue, Cambridge, CB2 0QH, United Kingdom
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  fullname: Horil Roy, Deeptee
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– sequence: 7
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  fullname: Joerger, Andreas C.
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– sequence: 8
  givenname: Alan R.
  surname: Fersht
  fullname: Fersht, Alan R.
  email: arf25@cam.ac.uk, alan@mrc-lmb.cam.ac.uk
  organization: Medical Research Council, Laboratory of Molecular Biology, Francis Crick Avenue, Cambridge, CB2 0QH, United Kingdom
BackLink https://www.ncbi.nlm.nih.gov/pubmed/29702446$$D View this record in MEDLINE/PubMed
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Copyright © 2018 MRC Laboratory of Molecular Biology. Published by Elsevier Masson SAS.. All rights reserved.
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ISSN 0223-5234
1768-3254
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Keywords Anticancer therapy
Structure-based drug discovery
Mutant p53
WILD-TYPE
DNA-BINDING
DESIGN
PROTEIN
TP53 MUTATION
GLIDE
CORE DOMAIN
RESCUE
ACCURATE DOCKING
REACTIVATION
Language English
License This is an open access article under the CC BY license.
Copyright © 2018 MRC Laboratory of Molecular Biology. Published by Elsevier Masson SAS.. All rights reserved.
This is an open access article under the CC BY license (http://creativecommons.org/licenses/by/4.0/).
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Notes researchfish
UKRI
European Research Council (ERC)
ObjectType-Article-1
SourceType-Scholarly Journals-1
ObjectType-Feature-2
content type line 23
These authors contributed equally.
ORCID 0000-0003-3714-4350
0000-0003-4015-6483
0000-0002-1232-0138
OpenAccessLink https://pubmed.ncbi.nlm.nih.gov/PMC5986712
PMID 29702446
PQID 2032403654
PQPubID 23479
PageCount 14
ParticipantIDs pubmedcentral_primary_oai_pubmedcentral_nih_gov_5986712
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PublicationTitle European journal of medicinal chemistry
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Snippet Many cancers have the tumor suppressor p53 inactivated by mutation, making reactivation of mutant p53 with small molecules a promising strategy for the...
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SubjectTerms Anticancer therapy
Antineoplastic Agents - chemical synthesis
Antineoplastic Agents - chemistry
Antineoplastic Agents - pharmacology
Benzothiazoles - chemical synthesis
Benzothiazoles - chemistry
Benzothiazoles - pharmacology
Cell Proliferation - drug effects
Cell Survival - drug effects
Chemistry, Medicinal
Dose-Response Relationship, Drug
Drug Screening Assays, Antitumor
Humans
Life Sciences & Biomedicine
Molecular Structure
Mutant p53
Pharmacology & Pharmacy
Real-Time Polymerase Chain Reaction
Science & Technology
Signal Transduction - drug effects
Signal Transduction - genetics
Structure-Activity Relationship
Structure-based drug discovery
Tumor Cells, Cultured
Tumor Suppressor Protein p53 - genetics
Tumor Suppressor Protein p53 - metabolism
Title Aminobenzothiazole derivatives stabilize the thermolabile p53 cancer mutant Y220C and show anticancer activity in p53-Y220C cell lines
URI https://dx.doi.org/10.1016/j.ejmech.2018.04.035
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https://www.ncbi.nlm.nih.gov/pubmed/29702446
https://www.proquest.com/docview/2032403654
https://pubmed.ncbi.nlm.nih.gov/PMC5986712
Volume 152
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