Evidence map›Paper›PMID 26414808›Full record

ArticleEuropean journal of medicinal chemistry2015

Ligand binding studies, preliminary structure-activity relationship and detailed mechanistic characterization of 1-phenyl-6,6-dimethyl-1,3,5-triazine-2,4-diamine derivatives as inhibitors of Escherichia coli dihydrofolate reductase.

Bharath Srinivasan, Sam Tonddast-Navaei, Jeffrey Skolnick

Open access · greenAbstract read
In one paragraph

Article in European journal of medicinal chemistry, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.

0numbers the graph read from it
0cells of the map it votes in
11citing papers in PubMed
1.9field-weighted citation impact, top 16% of its field
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

11 citing papers in PubMed, 23 citations in OpenAlex.

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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

3 authors at 1 institution in 1 country.

Bharath SrinivasanCenter for the Study of Systems Biology, School of Biology, Georgia Institute of Technology, 950, Atlantic Drive, Atlanta, GA 30332, United States. Electronic address: bharath.srinivasan@biology.gatech.edu.
Sam Tonddast-NavaeiCenter for the Study of Systems Biology, School of Biology, Georgia Institute of Technology, 950, Atlantic Drive, Atlanta, GA 30332, United States. Electronic address: sam.tonddastnavaei@biology.gatech.edu.
Jeffrey SkolnickCenter for the Study of Systems Biology, School of Biology, Georgia Institute of Technology, 950, Atlantic Drive, Atlanta, GA 30332, United States. Electronic address: skolnick@gatech.edu.
Georgia Institute of Technology · US

Funding

Interaction Pattern Based Predictor of Protein StruturesR01GM048835 · NIGMS · STATE UNIVERSITY OF NEW YORK AT BUFFALO · PI SKOLNICK, JEFFREY · 1994 to 2015
$4.0M
THEORY OF FOLDING TRANSITIONS IN A-HELICAL PROTEINSR01GM037408 · NIGMS · WASHINGTON UNIVERSITY · PI SKOLNICK, JEFFREY · 1987 to 2014
$3.9M
NIGMS NIH HHS GM-37408NIGMS NIH HHS GM-48835NIGMS NIH HHS R01 GM037408NIGMS NIH HHS R01 GM048835
6 · The paper itself

Abstract

Gram-negative bacteria are implicated in the causation of life-threatening hospital-acquired infections. They acquire rapid resistance to multiple drugs and available antibiotics. Hence, there is the need to discover new antibacterial agents with novel scaffolds. For the first time, this study explores the 1,3,5-triazine-2,4-diamine and 1,2,4-triazine-2,4-diamine group of compounds as potential inhibitors of Escherichia coli DHFR, a pivotal enzyme in the thymidine and purine synthesis pathway. Using differential scanning fluorimetry, DSF, fifteen compounds with various substitutions on either the 3rd or 4th positions on the benzene group of 6,6-dimethyl-1-(benzene)-1,3,5-triazine-2,4-diamine were shown to bind to the enzyme with varying affinities. Then, the dose dependence of inhibition by these compounds was determined. Preliminary quantitative structure-activity relationship analysis and docking studies implicate the alkyl linker group and the sulfonyl fluoride group in increasing the potency of inhibition. 4-[4-[3-(4,6-diamino-2,2-dimethyl-1,3,5-triazin-1-yl)phenyl]butyl]benzenesulfonyl fluoride (NSC120927), the best hit from the study and a molecule with no reported inhibition of E. coli DHFR, potently inhibits the enzyme with a Ki value of 42.50 ± 5.34 nM, followed by 4-[6-[4-(4,6-diamino-2,2-dimethyl-1,3,5-triazin-1-yl)phenyl]hexyl]benzenesulfonyl fluoride (NSC132279), with a Ki value of 100.9 ± 12.7 nM. Detailed kinetic characterization of the inhibition brought about by five small-molecule hits shows that these inhibitors bind to the dihydrofolate binding site with preferential binding to the NADPH-bound binary form of the enzyme. Furthermore, in search of novel diaminotriazine scaffolds, it is shown that lamotrigine, a 1,2,4-triazine-3,5-diamine and a sodium-ion channel blocker class of antiepileptic drug, also inhibits E. coli DHFR. This is the first comprehensive study on the binding and inhibition brought about by diaminotriazines of a gram-negative prokaryotic enzyme and provides valuable insights into the SAR as an aid to the discovery of novel antibiotics.

Indexed as

Binding SitesDose-Response Relationship, DrugEscherichia coliFolic Acid AntagonistsLigandsMolecular StructureStructure-Activity RelationshipSulfonesTetrahydrofolate DehydrogenaseTriazinesFolic Acid AntagonistsLigandsNSC120927SulfonesTetrahydrofolate DehydrogenaseTriazines2,4-Diamino 1,2,4-triazine2,4-Diamino-1,3,5-triazineDrug discoveryEscherichia coli dihydrofolate reductaseInhibition kineticsMechanistic characterizationQSAR

Identifiers

PMID26414808
PMCPMC4610388
OpenAlexW1254634972

What OpenQuestion holds

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Registered trials

None linked

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.