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The first biologically active synthetic analogues of FK228, the depsipeptide histone deacetylase inhibitor

The first biologically active synthetic analogues of FK228, the depsipeptide histone deacetylase inhibitor
The first biologically active synthetic analogues of FK228, the depsipeptide histone deacetylase inhibitor
The FK228 and spiruchostatin bicyclic depsipeptide natural products are among the most potent histone deacetylase (HDAC) inhibitors known. Although FK228 is in advanced clinical trials, the complexity of the natural products has precluded mechanistic studies and the discovery of structure-activity relationships. By total synthesis, we have prepared the first depsipeptide analogues. Our results prove that the dehydrobutyrine residue in FK228 is not essential, and other residues can be substituted without loss of HDAC inhibitory activity. Conformational restriction by the macrocyclic scaffold is important, as a linear peptide was inactive. The intramolecular disulfide formed with a cysteine side chain can be removed provided the zinc-binding thiol is protected to ensure good cellular availability. Like the natural products, the analogues are selective against class I isoforms, with nanomolar inhibition of class I HDAC1 and significantly less potency against class II HDAC6
natural products, time, spiruchostatin-a, modifying enzymes, potent, azumamide-e, inhibitor, epigenetic code, natural-products, chromobacterium-violaceum no-968, clinical trials, trial, identification, cancer, peptide, fr901228
0022-2623
5720-5726
Yurek-George, Alexander
bf3e1ac0-1459-4c95-93da-d7adba966f39
Cecil, Alexander Richard Liam
0b72e2b5-c24c-4d87-bc16-67c9eca7fe95
Mo, Alex Hon Kit
ba1645a5-8863-48a1-9a8a-4a2041952f5c
Wen, Shijun
8cdc63b3-e67c-4c03-b281-3639fb3015bd
Rogers, Helen
34f7ee40-8492-4cc6-b649-9f65e383a54d
Habens, Fay
3e4cce4b-4521-4702-9582-f817d25aad37
Maeda, Satoko
0f272d44-bfab-4972-80ee-8c17310f495f
Yoshida, Minoru
44c48a95-7a92-492a-97cf-520ab88869bc
Packham, Graham
fdabe56f-2c58-469c-aadf-38878f233394
Ganesan, A.
62aa5a87-9308-4383-8686-99726b6bcfb9
Yurek-George, Alexander
bf3e1ac0-1459-4c95-93da-d7adba966f39
Cecil, Alexander Richard Liam
0b72e2b5-c24c-4d87-bc16-67c9eca7fe95
Mo, Alex Hon Kit
ba1645a5-8863-48a1-9a8a-4a2041952f5c
Wen, Shijun
8cdc63b3-e67c-4c03-b281-3639fb3015bd
Rogers, Helen
34f7ee40-8492-4cc6-b649-9f65e383a54d
Habens, Fay
3e4cce4b-4521-4702-9582-f817d25aad37
Maeda, Satoko
0f272d44-bfab-4972-80ee-8c17310f495f
Yoshida, Minoru
44c48a95-7a92-492a-97cf-520ab88869bc
Packham, Graham
fdabe56f-2c58-469c-aadf-38878f233394
Ganesan, A.
62aa5a87-9308-4383-8686-99726b6bcfb9

Yurek-George, Alexander, Cecil, Alexander Richard Liam, Mo, Alex Hon Kit, Wen, Shijun, Rogers, Helen, Habens, Fay, Maeda, Satoko, Yoshida, Minoru, Packham, Graham and Ganesan, A. (2007) The first biologically active synthetic analogues of FK228, the depsipeptide histone deacetylase inhibitor. Journal of Medicinal Chemistry, 50 (23), 5720-5726. (doi:10.1021/jm0703800).

Record type: Article

Abstract

The FK228 and spiruchostatin bicyclic depsipeptide natural products are among the most potent histone deacetylase (HDAC) inhibitors known. Although FK228 is in advanced clinical trials, the complexity of the natural products has precluded mechanistic studies and the discovery of structure-activity relationships. By total synthesis, we have prepared the first depsipeptide analogues. Our results prove that the dehydrobutyrine residue in FK228 is not essential, and other residues can be substituted without loss of HDAC inhibitory activity. Conformational restriction by the macrocyclic scaffold is important, as a linear peptide was inactive. The intramolecular disulfide formed with a cysteine side chain can be removed provided the zinc-binding thiol is protected to ensure good cellular availability. Like the natural products, the analogues are selective against class I isoforms, with nanomolar inhibition of class I HDAC1 and significantly less potency against class II HDAC6

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More information

Published date: 15 November 2007
Keywords: natural products, time, spiruchostatin-a, modifying enzymes, potent, azumamide-e, inhibitor, epigenetic code, natural-products, chromobacterium-violaceum no-968, clinical trials, trial, identification, cancer, peptide, fr901228

Identifiers

Local EPrints ID: 62976
URI: http://eprints.soton.ac.uk/id/eprint/62976
ISSN: 0022-2623
PURE UUID: 39d3f16d-d79d-4692-8f64-1329163202f6
ORCID for Graham Packham: ORCID iD orcid.org/0000-0002-9232-5691

Catalogue record

Date deposited: 11 Sep 2008
Last modified: 16 Mar 2024 03:14

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Contributors

Author: Alexander Yurek-George
Author: Alexander Richard Liam Cecil
Author: Alex Hon Kit Mo
Author: Shijun Wen
Author: Helen Rogers
Author: Fay Habens
Author: Satoko Maeda
Author: Minoru Yoshida
Author: Graham Packham ORCID iD
Author: A. Ganesan

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