Evidence map›Paper›PMID 34010508›Full record

ArticleChemMedChem2021

Structure-Activity Relationship and Mode-Of-Action Studies Highlight 1-(4-Biphenylylmethyl)-1H-imidazole-Derived Small Molecules as Potent CYP121 Inhibitors.

Isabell Walter, Sebastian Adam, Maria Virginia Gentilini, Andreas M Kany, Christian Brengel, Andreas Thomann, Tim Sparwasser, Jesko Köhnke, Rolf W Hartmann

Abstract read
In one paragraph

Article in ChemMedChem, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 6 papers.

0numbers the graph read from it
0cells of the map it votes in
6citing papers in PubMed
–field-weighted citation impact
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

6 citing papers in PubMed.

  1. Article
  2. Structure-Function Analysis of the EssentialInternational journal of molecular sciences · 2024
    Article
  3. Review
  4. Article
  5. Article
  6. Article
4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

9 authors.

Isabell WalterDepartment for Drug Design and Optimization, Helmholtz Institute for Pharmaceutical Research Saarland, Campus E8.1, 66123, Saarbrücken, Germany.
Sebastian AdamWorkgroup Structural Biology of Biosynthetic Enzymes, Helmholtz Institute for Pharmaceutical Research Saarland (HIPS), Helmholtz Centre for Infection Research (HZI), Saarland University, Saarbrücken, Germany.ORCID 0000-0003-3319-6356
Maria Virginia GentiliniInstitute of Infection Immunology, TWINCORE, Centre for Experimental and Clinical Infection Research, A Joint Venture between the Medical School Hannover (MHH) and the Helmholtz Centre for Infection Research (HZI), Hannover, Germany.
Andreas M KanyDepartment for Drug Design and Optimization, Helmholtz Institute for Pharmaceutical Research Saarland, Campus E8.1, 66123, Saarbrücken, Germany.ORCID 0000-0001-7580-3658
Christian BrengelDepartment for Drug Design and Optimization, Helmholtz Institute for Pharmaceutical Research Saarland, Campus E8.1, 66123, Saarbrücken, Germany.
Andreas ThomannDepartment for Drug Design and Optimization, Helmholtz Institute for Pharmaceutical Research Saarland, Campus E8.1, 66123, Saarbrücken, Germany.
Tim SparwasserInstitute of Infection Immunology, TWINCORE, Centre for Experimental and Clinical Infection Research, A Joint Venture between the Medical School Hannover (MHH) and the Helmholtz Centre for Infection Research (HZI), Hannover, Germany.ORCID 0000-0001-5645-902X
Jesko KöhnkeWorkgroup Structural Biology of Biosynthetic Enzymes, Helmholtz Institute for Pharmaceutical Research Saarland (HIPS), Helmholtz Centre for Infection Research (HZI), Saarland University, Saarbrücken, Germany.ORCID 0000-0002-7153-1365
Rolf W HartmannDepartment for Drug Design and Optimization, Helmholtz Institute for Pharmaceutical Research Saarland, Campus E8.1, 66123, Saarbrücken, Germany.

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

CYP121 of Mycobacterium tuberculosis (Mtb) is an essential target for the development of novel potent drugs against tuberculosis (TB). Besides known antifungal azoles, further compounds of the azole class were recently identified as CYP121 inhibitors with antimycobacterial activity. Herein, we report the screening of a similarity-oriented library based on the former hit compound, the evaluation of affinity toward CYP121, and activity against M. bovis BCG. The results enabled a comprehensive SAR study, which was extended through the synthesis of promising compounds and led to the identification of favorable features for affinity and/or activity and hit compounds with 2.7-fold improved potency. Mode of action studies show that the hit compounds inhibit substrate conversion and highlighted CYP121 as the main antimycobacterial target of our compounds. Exemplified complex crystal structures of CYP121 with three inhibitors reveal a common binding site. Engaging in both hydrophobic interactions as well as hydrogen bonding to the sixth iron ligand, our compounds block a solvent channel leading to the active site heme. Additionally, we report the first CYP inhibitors that are able to reduce the intracellular replication of M. bovis BCG in macrophages, emphasizing their potential as future drug candidates against TB.

Indexed as

Antitubercular AgentsCytochrome P-450 Enzyme InhibitorsCytochrome P-450 Enzyme SystemDose-Response Relationship, DrugImidazolesMicrobial Sensitivity TestsMolecular StructureMycobacterium tuberculosisSmall Molecule LibrariesStructure-Activity RelationshipAntitubercular Agentscytochrome P-450 CYP121Cytochrome P-450 Enzyme InhibitorsCytochrome P-450 Enzyme SystemImidazolesSmall Molecule Librariesbiological activitycomplex structuresCYP121Mycobacterium tuberculosisstructure-activity relationships

Identifiers

PMID34010508
PMCPMC8519103

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Registered trials

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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.