Evidence map›Paper›PMID 32093094›Full record

ArticleMolecules (Basel, Switzerland)2020

Efficient Biocatalytic Synthesis of Dihalogenated Purine Nucleoside Analogues Applying Thermodynamic Calculations.

Heba Yehia, Sarah Westarp, Viola Röhrs, Felix Kaspar, Robert T Giessmann, Hendrik F T Klare, Katharina Paulick, Peter Neubauer, Jens Kurreck, Anke Wagner

Open access · goldAbstract read
In one paragraph

Article in Molecules (Basel, Switzerland), 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.

0numbers the graph read from it
0cells of the map it votes in
9citing papers in PubMed
1.5field-weighted citation impact, top 18% 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

9 citing papers in PubMed, 24 citations in OpenAlex.

  1. Review
  2. Production of Modified Nucleosides in a Continuous Enzyme Membrane Reactor.International journal of molecular sciences · 2023
    Article
  3. Optimized Biocatalytic Synthesis of 2-Selenopyrimidine Nucleosides by Transglycosylation*.Chembiochem : a European journal of chemical biology · 2021
    Article
  4. Article
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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

10 authors at 2 institutions in 2 countries.

Heba YehiaChair of Bioprocess Engineering, Faculty III Process Sciences, Institute of Biotechnology, Technische Universität Berlin, Straße des 17. Juni 135, 10623 Berlin, Germany.ORCID 0000-0002-3238-0939
Sarah WestarpChair of Bioprocess Engineering, Faculty III Process Sciences, Institute of Biotechnology, Technische Universität Berlin, Straße des 17. Juni 135, 10623 Berlin, Germany.ORCID 0000-0001-6498-8810
Viola RöhrsChair of Applied Biochemistry, Faculty III Process Sciences, Institute of Biotechnology, Technische Universität Berlin, Straße des 17. Juni 135, 10623 Berlin, Germany.
Felix KasparChair of Bioprocess Engineering, Faculty III Process Sciences, Institute of Biotechnology, Technische Universität Berlin, Straße des 17. Juni 135, 10623 Berlin, Germany.ORCID 0000-0001-6391-043X
Robert T GiessmannChair of Bioprocess Engineering, Faculty III Process Sciences, Institute of Biotechnology, Technische Universität Berlin, Straße des 17. Juni 135, 10623 Berlin, Germany.ORCID 0000-0002-0254-1500
Hendrik F T KlareFaculty II Mathematics and Natural Sciences, Institute of Chemistry, Technische Universität Berlin, Strasse des 17. Juni 135, 10623 Berlin, Germany.ORCID 0000-0003-3748-6609
Katharina PaulickChair of Bioprocess Engineering, Faculty III Process Sciences, Institute of Biotechnology, Technische Universität Berlin, Straße des 17. Juni 135, 10623 Berlin, Germany.
Peter NeubauerChair of Bioprocess Engineering, Faculty III Process Sciences, Institute of Biotechnology, Technische Universität Berlin, Straße des 17. Juni 135, 10623 Berlin, Germany.ORCID 0000-0002-1214-9713
Jens KurreckChair of Applied Biochemistry, Faculty III Process Sciences, Institute of Biotechnology, Technische Universität Berlin, Straße des 17. Juni 135, 10623 Berlin, Germany.ORCID 0000-0002-1469-0052
Anke WagnerChair of Bioprocess Engineering, Faculty III Process Sciences, Institute of Biotechnology, Technische Universität Berlin, Straße des 17. Juni 135, 10623 Berlin, Germany.ORCID 0000-0001-6919-725X
Technische Universität Berlin · DENational Research Centre · EG

Funding

Deutsche Forschungsgemeinschaft 390540038
6 · The paper itself

Abstract

The enzymatic synthesis of nucleoside analogues has been shown to be a sustainable and efficient alternative to chemical synthesis routes. In this study, dihalogenated nucleoside analogues were produced by thermostable nucleoside phosphorylases in transglycosylation reactions using uridine or thymidine as sugar donors. Prior to the enzymatic process, ideal maximum product yields were calculated after the determination of equilibrium constants through monitoring the equilibrium conversion in analytical-scale reactions. Equilibrium constants for dihalogenated nucleosides were comparable to known purine nucleosides, ranging between 0.071 and 0.081. To achieve 90% product yield in the enzymatic process, an approximately five-fold excess of sugar donor was needed. Nucleoside analogues were purified by semi-preparative HPLC, and yields of purified product were approximately 50% for all target compounds. To evaluate the impact of halogen atoms in positions 2 and 6 on the antiproliferative activity in leukemic cell lines, the cytotoxic potential of dihalogenated nucleoside analogues was studied in the leukemic cell line HL-60. Interestingly, the inhibition of HL-60 cells with dihalogenated nucleoside analogues was substantially lower than with monohalogenated cladribine, which is known to show high antiproliferative activity. Taken together, we demonstrate that thermodynamic calculations and small-scale experiments can be used to produce nucleoside analogues with high yields and purity on larger scales. The procedure can be used for the generation of new libraries of nucleoside analogues for screening experiments or to replace the chemical synthesis routes of marketed nucleoside drugs by enzymatic processes.

Indexed as

Antineoplastic AgentsHydrocarbons, HalogenatedPurine NucleosidesHL-60 CellsHumansLeukemiaPentosyltransferasesThermodynamicsAntineoplastic AgentsHydrocarbons, Halogenatednucleoside phosphorylasePentosyltransferasesPurine Nucleosidescytostaticsdihalogenated nucleoside analogueleukemic cell linethermodynamic calculationsthermostable nucleoside phosphorylaseyield prediction

Identifiers

PMID32093094
PMCPMC7070685
OpenAlexW3008253371

What OpenQuestion holds

Textmetadata
LicenceCC BY
Read underepoch 390

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.