Design and synthesis of mycobacterial pks13 inhibitors: Conformationally rigid tetracyclic molecules

We previously reported a series of coumestans−a naturally occurring tetracyclic scaffold containing a δ-lactone−that effectively target the thioesterase domain of polyketide synthase 13 (Pks13) in Mycobacterium tuberculosis (Mtb), resulting in superior anti-tuberculosis (TB) activity. Compared to th...

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Main Authors: Zhang, W., Liu, L.L., Lun, S., Wang, S.S., Xiao, S., Gunosewoyo, Hendra, Yang, F., Tang, J., Bishai, W.R., Yu, L.F.
Format: Journal Article
Language:English
Published: ELSEVIER FRANCE-EDITIONS SCIENTIFIQUES MEDICALES ELSEVIER 2021
Subjects:
Online Access:http://purl.org/au-research/grants/arc/DE160100482
http://hdl.handle.net/20.500.11937/90987
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author Zhang, W.
Liu, L.L.
Lun, S.
Wang, S.S.
Xiao, S.
Gunosewoyo, Hendra
Yang, F.
Tang, J.
Bishai, W.R.
Yu, L.F.
author_facet Zhang, W.
Liu, L.L.
Lun, S.
Wang, S.S.
Xiao, S.
Gunosewoyo, Hendra
Yang, F.
Tang, J.
Bishai, W.R.
Yu, L.F.
author_sort Zhang, W.
building Curtin Institutional Repository
collection Online Access
description We previously reported a series of coumestans−a naturally occurring tetracyclic scaffold containing a δ-lactone−that effectively target the thioesterase domain of polyketide synthase 13 (Pks13) in Mycobacterium tuberculosis (Mtb), resulting in superior anti-tuberculosis (TB) activity. Compared to the corresponding ‘open-form’ ethyl benzofuran-3-carboxylates, the enhanced anti-TB effects seen with the conformationally restricted coumestan series could be attributed to the extra π-π stacking interactions between the benzene ring of coumestans and the phenyl ring of F1670 residue located in the Pks13-TE binding domain. To further probe this binding feature, novel tetracyclic analogues were synthesized and evaluated for their anti-TB activity against the Mtb strain H37Rv. Initial comparison of the ‘open-form’ analogueues against the tetracyclic counterparts again showed that the latter is superior in terms of anti-TB activity. In particular, the δ-lactam-containing 5H-benzofuro [3,2-c]quinolin-6-ones gave the most promising results. Compound 65 demonstrated potent activity against Mtb H37Rv with MIC value between 0.0313 and 0.0625 μg/mL, with high selectivity to Vero cells (64–128 fold). The thermal stability analysis supports the notion that the tetracyclic compounds bind to the Pks13-TE domain as measured by nano DSF, consistent with the observed SAR trends. Compound 65 also showed excellent selectivity against actinobacteria and therefore unlikely to develop potential drug resistance to nonpathogenic bacteria.
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institution Curtin University Malaysia
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language English
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spelling curtin-20.500.11937-909872023-05-24T01:07:52Z Design and synthesis of mycobacterial pks13 inhibitors: Conformationally rigid tetracyclic molecules Zhang, W. Liu, L.L. Lun, S. Wang, S.S. Xiao, S. Gunosewoyo, Hendra Yang, F. Tang, J. Bishai, W.R. Yu, L.F. Science & Technology Life Sciences & Biomedicine Chemistry, Medicinal Pharmacology & Pharmacy Polyketide synthase 13 conformationally rigid tetracyclics Antitubercular agents Antitubercular agents Polyketide synthase 13 conformationally rigid tetracyclics Antitubercular Agents Bacterial Proteins Dose-Response Relationship, Drug Drug Design Enzyme Inhibitors Microbial Sensitivity Tests Models, Molecular Molecular Structure Mycobacterium tuberculosis Polyketide Synthases Quinolones Structure-Activity Relationship Mycobacterium tuberculosis Quinolones Polyketide Synthases Bacterial Proteins Enzyme Inhibitors Antitubercular Agents Microbial Sensitivity Tests Molecular Structure Structure-Activity Relationship Dose-Response Relationship, Drug Drug Design Models, Molecular We previously reported a series of coumestans−a naturally occurring tetracyclic scaffold containing a δ-lactone−that effectively target the thioesterase domain of polyketide synthase 13 (Pks13) in Mycobacterium tuberculosis (Mtb), resulting in superior anti-tuberculosis (TB) activity. Compared to the corresponding ‘open-form’ ethyl benzofuran-3-carboxylates, the enhanced anti-TB effects seen with the conformationally restricted coumestan series could be attributed to the extra π-π stacking interactions between the benzene ring of coumestans and the phenyl ring of F1670 residue located in the Pks13-TE binding domain. To further probe this binding feature, novel tetracyclic analogues were synthesized and evaluated for their anti-TB activity against the Mtb strain H37Rv. Initial comparison of the ‘open-form’ analogueues against the tetracyclic counterparts again showed that the latter is superior in terms of anti-TB activity. In particular, the δ-lactam-containing 5H-benzofuro [3,2-c]quinolin-6-ones gave the most promising results. Compound 65 demonstrated potent activity against Mtb H37Rv with MIC value between 0.0313 and 0.0625 μg/mL, with high selectivity to Vero cells (64–128 fold). The thermal stability analysis supports the notion that the tetracyclic compounds bind to the Pks13-TE domain as measured by nano DSF, consistent with the observed SAR trends. Compound 65 also showed excellent selectivity against actinobacteria and therefore unlikely to develop potential drug resistance to nonpathogenic bacteria. 2021 Journal Article http://hdl.handle.net/20.500.11937/90987 10.1016/j.ejmech.2021.113202 English http://purl.org/au-research/grants/arc/DE160100482 http://creativecommons.org/licenses/by-nc-nd/4.0/ ELSEVIER FRANCE-EDITIONS SCIENTIFIQUES MEDICALES ELSEVIER fulltext
spellingShingle Science & Technology
Life Sciences & Biomedicine
Chemistry, Medicinal
Pharmacology & Pharmacy
Polyketide synthase 13
conformationally rigid tetracyclics
Antitubercular agents
Antitubercular agents
Polyketide synthase 13
conformationally rigid tetracyclics
Antitubercular Agents
Bacterial Proteins
Dose-Response Relationship, Drug
Drug Design
Enzyme Inhibitors
Microbial Sensitivity Tests
Models, Molecular
Molecular Structure
Mycobacterium tuberculosis
Polyketide Synthases
Quinolones
Structure-Activity Relationship
Mycobacterium tuberculosis
Quinolones
Polyketide Synthases
Bacterial Proteins
Enzyme Inhibitors
Antitubercular Agents
Microbial Sensitivity Tests
Molecular Structure
Structure-Activity Relationship
Dose-Response Relationship, Drug
Drug Design
Models, Molecular
Zhang, W.
Liu, L.L.
Lun, S.
Wang, S.S.
Xiao, S.
Gunosewoyo, Hendra
Yang, F.
Tang, J.
Bishai, W.R.
Yu, L.F.
Design and synthesis of mycobacterial pks13 inhibitors: Conformationally rigid tetracyclic molecules
title Design and synthesis of mycobacterial pks13 inhibitors: Conformationally rigid tetracyclic molecules
title_full Design and synthesis of mycobacterial pks13 inhibitors: Conformationally rigid tetracyclic molecules
title_fullStr Design and synthesis of mycobacterial pks13 inhibitors: Conformationally rigid tetracyclic molecules
title_full_unstemmed Design and synthesis of mycobacterial pks13 inhibitors: Conformationally rigid tetracyclic molecules
title_short Design and synthesis of mycobacterial pks13 inhibitors: Conformationally rigid tetracyclic molecules
title_sort design and synthesis of mycobacterial pks13 inhibitors: conformationally rigid tetracyclic molecules
topic Science & Technology
Life Sciences & Biomedicine
Chemistry, Medicinal
Pharmacology & Pharmacy
Polyketide synthase 13
conformationally rigid tetracyclics
Antitubercular agents
Antitubercular agents
Polyketide synthase 13
conformationally rigid tetracyclics
Antitubercular Agents
Bacterial Proteins
Dose-Response Relationship, Drug
Drug Design
Enzyme Inhibitors
Microbial Sensitivity Tests
Models, Molecular
Molecular Structure
Mycobacterium tuberculosis
Polyketide Synthases
Quinolones
Structure-Activity Relationship
Mycobacterium tuberculosis
Quinolones
Polyketide Synthases
Bacterial Proteins
Enzyme Inhibitors
Antitubercular Agents
Microbial Sensitivity Tests
Molecular Structure
Structure-Activity Relationship
Dose-Response Relationship, Drug
Drug Design
Models, Molecular
url http://purl.org/au-research/grants/arc/DE160100482
http://hdl.handle.net/20.500.11937/90987