Human telomerase inhibition by substituted acridine derivatives

A series of 3,6-disubstituted acridine derivatives have been rationally designed as telomerase inhibitors. They have been designed on the basis that inhibition of telomerase occurs by stabilising G-quadruplex structures formed by the folding of telomeric DNA. The most potent inhibitors have IC 50 va...

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Veröffentlicht in:	Bioorganic & medicinal chemistry letters Jg. 9; H. 17; S. 2463 - 2468
Hauptverfasser:	Harrison, R. John, Gowan, Sharon M., Kelland, Lloyd R., Neidle, Stephen
Format:	Journal Article
Sprache:	Englisch
Veröffentlicht:	Oxford Elsevier Ltd 06.09.1999 Elsevier
Schlagworte:	Acridines - chemistry Acridines - pharmacology Antineoplastic agents Antineoplastic Agents - chemistry Antineoplastic Agents - pharmacology Biological and medical sciences Drug Screening Assays, Antitumor Enzyme Inhibitors - chemistry Enzyme Inhibitors - pharmacology General aspects Humans Medical sciences Pharmacology. Drug treatments Telomerase - antagonists & inhibitors Tumor Cells, Cultured Antineoplastic agent Human Enzyme Aminoamide Nitrogen heterocycle Transferases Acridine derivatives Enzyme inhibitor Cytotoxicity Tricyclic compound In vitro Ovary Nucleotidyltransferases Cell line Structure activity relation Tertiary amine Aromatic compound Chemical synthesis DNA-directed DNA polymerase
ISSN:	0960-894X, 1464-3405
Online-Zugang:	Volltext
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Abstract	A series of 3,6-disubstituted acridine derivatives have been rationally designed as telomerase inhibitors. They have been designed on the basis that inhibition of telomerase occurs by stabilising G-quadruplex structures formed by the folding of telomeric DNA. The most potent inhibitors have IC 50 values against telomerase of between 1.3 and 8 μM, comparable to their cytotoxicity in ovarian cancer cell lines.
AbstractList	A series of 3,6-disubstituted acridine derivatives have been rationally designed as telomerase inhibitors. They have been designed on the basis that inhibition of telomerase occurs by stabilising G-quadruplex structures formed by the folding of telomeric DNA. The most potent inhibitors have IC 50 values against telomerase of between 1.3 and 8 μM, comparable to their cytotoxicity in ovarian cancer cell lines. A series of 3,6-disubstituted acridine derivatives have been rationally designed as telomerase inhibitors. They have been designed on the basis that inhibition of telomerase occurs by stabilising G-quadruplex structures formed by the folding of telomeric DNA. The most potent inhibitors have IC50 values against telomerase of between 1.3 and 8 microM, comparable to their cytotoxicity in ovarian cancer cell lines.A series of 3,6-disubstituted acridine derivatives have been rationally designed as telomerase inhibitors. They have been designed on the basis that inhibition of telomerase occurs by stabilising G-quadruplex structures formed by the folding of telomeric DNA. The most potent inhibitors have IC50 values against telomerase of between 1.3 and 8 microM, comparable to their cytotoxicity in ovarian cancer cell lines. A series of 3,6-disubstituted acridine derivatives have been rationally designed as telomerase inhibitors. They have been designed on the basis that inhibition of telomerase occurs by stabilising G-quadruplex structures formed by the folding of telomeric DNA. The most potent inhibitors have IC50 values against telomerase of between 1.3 and 8 microM, comparable to their cytotoxicity in ovarian cancer cell lines.
Author	Neidle, Stephen Kelland, Lloyd R. Gowan, Sharon M. Harrison, R. John
Author_xml	– sequence: 1 givenname: R. John surname: Harrison fullname: Harrison, R. John organization: CRC Biomolecular Structure Unit, The Institute of Cancer Research, Sutton, Surrey SM2 5NG, U.K – sequence: 2 givenname: Sharon M. surname: Gowan fullname: Gowan, Sharon M. organization: CRC Centre for Cancer Therapeutics, The Institute of Cancer Research, Sutton, Surrey SM2 5NG, U.K – sequence: 3 givenname: Lloyd R. surname: Kelland fullname: Kelland, Lloyd R. organization: CRC Centre for Cancer Therapeutics, The Institute of Cancer Research, Sutton, Surrey SM2 5NG, U.K – sequence: 4 givenname: Stephen surname: Neidle fullname: Neidle, Stephen email: steve@iris5.icr.ac.uk organization: CRC Biomolecular Structure Unit, The Institute of Cancer Research, Sutton, Surrey SM2 5NG, U.K
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Keywords	Antineoplastic agent Human Enzyme Aminoamide Nitrogen heterocycle Transferases Acridine derivatives Enzyme inhibitor Cytotoxicity Tricyclic compound In vitro Ovary Nucleotidyltransferases Cell line Structure activity relation Tertiary amine Aromatic compound Chemical synthesis DNA-directed DNA polymerase
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Snippet	A series of 3,6-disubstituted acridine derivatives have been rationally designed as telomerase inhibitors. They have been designed on the basis that inhibition...
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SubjectTerms	Acridines - chemistry Acridines - pharmacology Antineoplastic agents Antineoplastic Agents - chemistry Antineoplastic Agents - pharmacology Biological and medical sciences Drug Screening Assays, Antitumor Enzyme Inhibitors - chemistry Enzyme Inhibitors - pharmacology General aspects Humans Medical sciences Pharmacology. Drug treatments Telomerase - antagonists & inhibitors Tumor Cells, Cultured
Title	Human telomerase inhibition by substituted acridine derivatives
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