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  1. Article ; Online: Towards More Practical Methods for the Chemical Synthesis of Thioamides Using Sulfuration Agents: A Decade Update.

    Zhang, Qiang / Soulère, Laurent / Queneau, Yves

    Molecules (Basel, Switzerland)

    2023  Volume 28, Issue 8

    Abstract: Compounds possessing a thioamide function play a crucial role in organic synthesis, serving as key building blocks. They are also important in the pharmaceutical chemistry and drug design, owing to their ability to mimic the amide function in ... ...

    Abstract Compounds possessing a thioamide function play a crucial role in organic synthesis, serving as key building blocks. They are also important in the pharmaceutical chemistry and drug design, owing to their ability to mimic the amide function in biomolecules while retaining or developing biological activity. From the synthetic viewpoint, several methods have been developed for preparing thioamides using sulfuration agents. The purpose of this review is to give an update of the last decade of contributions focusing on the formation of thioamides employing different sulfur sources. When appropriate, the cleanness and practicality of the new methods are highlighted.
    Language English
    Publishing date 2023-04-17
    Publishing country Switzerland
    Document type Journal Article ; Review
    ZDB-ID 1413402-0
    ISSN 1420-3049 ; 1431-5165 ; 1420-3049
    ISSN (online) 1420-3049
    ISSN 1431-5165 ; 1420-3049
    DOI 10.3390/molecules28083527
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    Zs.MO 81: Show issues

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  2. Article ; Online: In Silico Identification of Potential Inhibitors of the SARS-CoV-2 Main Protease among a PubChem Database of Avian Infectious Bronchitis Virus 3CLPro Inhibitors.

    Soulère, Laurent / Barbier, Thibaut / Queneau, Yves

    Biomolecules

    2023  Volume 13, Issue 6

    Abstract: Remarkable structural homologies between the main proteases of the severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) and the avian infectious bronchitis virus (IBV) were revealed by comparative amino-acid sequence and 3D structural alignment. ... ...

    Abstract Remarkable structural homologies between the main proteases of the severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) and the avian infectious bronchitis virus (IBV) were revealed by comparative amino-acid sequence and 3D structural alignment. Assessing whether reported IBV 3CLPro inhibitors could also interact with SARS-CoV-2 has been undertaken in silico using a PubChem BioAssay database of 388 compounds active on the avian infectious bronchitis virus 3C-like protease. Docking studies of this database on the SARS-CoV-2 protease resulted in the identification of four covalent inhibitors targeting the catalytic cysteine residue and five non-covalent inhibitors for which the binding was further investigated by molecular dynamics (MD) simulations. Predictive ADMET calculations on the nine compounds suggest promising pharmacokinetic properties.
    MeSH term(s) Humans ; SARS-CoV-2 ; COVID-19 ; Infectious bronchitis virus ; Molecular Docking Simulation ; Protease Inhibitors/pharmacology ; Protease Inhibitors/chemistry ; Coronavirus 3C Proteases ; Molecular Dynamics Simulation
    Chemical Substances 3C-like proteinase, SARS-CoV-2 (EC 3.4.22.-) ; Protease Inhibitors ; Coronavirus 3C Proteases (EC 3.4.22.28)
    Language English
    Publishing date 2023-06-07
    Publishing country Switzerland
    Document type Journal Article
    ZDB-ID 2701262-1
    ISSN 2218-273X ; 2218-273X
    ISSN (online) 2218-273X
    ISSN 2218-273X
    DOI 10.3390/biom13060956
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  3. Article ; Online: Importance of the 2,6-Difluorobenzamide Motif for FtsZ Allosteric Inhibition: Insights from Conformational Analysis, Molecular Docking and Structural Modifications.

    Barbier, Thibaut / Dumitrescu, Oana / Lina, Gérard / Queneau, Yves / Soulère, Laurent

    Molecules (Basel, Switzerland)

    2023  Volume 28, Issue 5

    Abstract: A conformational analysis and molecular docking study comparing 2,6-difluoro-3-methoxybenzamide (DFMBA) with 3-methoxybenzamide (3-MBA) has been undertaken for investigating the known increase of FtsZ inhibition related ... ...

    Abstract A conformational analysis and molecular docking study comparing 2,6-difluoro-3-methoxybenzamide (DFMBA) with 3-methoxybenzamide (3-MBA) has been undertaken for investigating the known increase of FtsZ inhibition related anti
    MeSH term(s) Molecular Docking Simulation ; Benzamides/chemistry ; Molecular Conformation ; Bacterial Proteins/chemistry
    Chemical Substances 2,6-difluorobenzamide (SJ2RN214MK) ; 3-methoxybenzamide (M8502TLK98) ; Benzamides ; Bacterial Proteins
    Language English
    Publishing date 2023-02-22
    Publishing country Switzerland
    Document type Journal Article
    ZDB-ID 1413402-0
    ISSN 1420-3049 ; 1431-5165 ; 1420-3049
    ISSN (online) 1420-3049
    ISSN 1431-5165 ; 1420-3049
    DOI 10.3390/molecules28052055
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  4. Article ; Online: Straightforward Synthesis of Chiral Terpenoid Building Blocks by Ru-Catalyzed Enantioselective Hydrogenation.

    Ruiz, Johal / Oger, Philippe / Soulère, Laurent / Popowycz, Florence

    The Journal of organic chemistry

    2021  Volume 86, Issue 14, Page(s) 9396–9406

    Abstract: Starting from commercially available ( ...

    Abstract Starting from commercially available (
    MeSH term(s) Alkenes ; Catalysis ; Hydrogenation ; Stereoisomerism ; Terpenes
    Chemical Substances Alkenes ; Terpenes
    Language English
    Publishing date 2021-06-28
    Publishing country United States
    Document type Journal Article ; Research Support, Non-U.S. Gov't
    ZDB-ID 123490-0
    ISSN 1520-6904 ; 0022-3263
    ISSN (online) 1520-6904
    ISSN 0022-3263
    DOI 10.1021/acs.joc.1c00677
    Database MEDical Literature Analysis and Retrieval System OnLINE

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    Zs.A 4473: Show issues Location:
    Je nach Verfügbarkeit (siehe Angabe bei Bestand)
    bis Jg. 1994: Bestellungen von Artikeln über das Online-Bestellformular
    Jg. 1995 - 2021: Lesesall (2.OG)
    ab Jg. 2022: Lesesaal (EG)

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  5. Article ; Online: Docking-based virtual screening studies aiming at the covalent inhibition of SARS-CoV-2 M

    Soulère, Laurent / Barbier, Thibaut / Queneau, Yves

    Computational biology and chemistry

    2021  Volume 92, Page(s) 107463

    Abstract: The severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) is responsible for the COVID-19 which has infected millions of people worldwide. The main protease of SARS-CoV-2 ( ... ...

    Abstract The severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) is responsible for the COVID-19 which has infected millions of people worldwide. The main protease of SARS-CoV-2 (M
    MeSH term(s) Amino Acid Sequence ; Antiviral Agents/chemistry ; Antiviral Agents/pharmacology ; Binding Sites ; COVID-19/drug therapy ; Coronavirus 3C Proteases/chemistry ; Cysteine/antagonists & inhibitors ; Cysteine/metabolism ; Drug Evaluation, Preclinical ; Humans ; Molecular Docking Simulation ; Protein Binding ; SARS-CoV-2/chemistry ; SARS-CoV-2/drug effects
    Chemical Substances Antiviral Agents ; Coronavirus 3C Proteases (EC 3.4.22.28) ; Cysteine (K848JZ4886)
    Language English
    Publishing date 2021-02-20
    Publishing country England
    Document type Journal Article
    ISSN 1476-928X
    ISSN (online) 1476-928X
    DOI 10.1016/j.compbiolchem.2021.107463
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  6. Article ; Online: Importance of the 2,6-Difluorobenzamide Motif for FtsZ Allosteric Inhibition

    Thibaut Barbier / Oana Dumitrescu / Gérard Lina / Yves Queneau / Laurent Soulère

    Molecules, Vol 28, Iss 2055, p

    Insights from Conformational Analysis, Molecular Docking and Structural Modifications

    2023  Volume 2055

    Abstract: A conformational analysis and molecular docking study comparing 2,6-difluoro-3-methoxybenzamide (DFMBA) with 3-methoxybenzamide (3-MBA) has been undertaken for investigating the known increase of FtsZ inhibition related anti S. aureus activity due to ... ...

    Abstract A conformational analysis and molecular docking study comparing 2,6-difluoro-3-methoxybenzamide (DFMBA) with 3-methoxybenzamide (3-MBA) has been undertaken for investigating the known increase of FtsZ inhibition related anti S. aureus activity due to fluorination. For the isolated molecules, the calculations reveal that the presence of the fluorine atoms in DFMBA is responsible for its non-planarity, with a dihedral angle of -27° between the carboxamide and the aromatic ring. When interacting with the protein, the fluorinated ligand can thus more easily adopt the non-planar conformation found in reported co-crystallized complexes with FtsZ, than the non-fluorinated one. Molecular docking studies of the favored non-planar conformation of 2,6-difluoro-3-methoxybenzamide highlights the strong hydrophobic interactions between the difluoroaromatic ring and several key residues of the allosteric pocket, precisely between the 2-fluoro substituent and residues Val203 and Val297 and between the 6-fluoro group and the residues Asn263. The docking simulation in the allosteric binding site also confirms the critical importance of the hydrogen bonds between the carboxamide group with the residues Val207, Leu209 and Asn263. Changing the carboxamide functional group of 3-alkyloxybenzamide and 3-alkyloxy-2,6-difluorobenzamide to a benzohydroxamic acid or benzohydrazide led to inactive compounds, confirming the importance of the carboxamide group.
    Keywords conformational analysis ; 2,6-difluorobenzamide ; FtsZ ; S. aureus ; Organic chemistry ; QD241-441
    Subject code 540
    Language English
    Publishing date 2023-02-01T00:00:00Z
    Publisher MDPI AG
    Document type Article ; Online
    Database BASE - Bielefeld Academic Search Engine (life sciences selection)

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  7. Article ; Online: Conformational and docking studies of acyl homoserine lactones as a robust method to investigate bioactive conformations.

    Soulère, Laurent / Queneau, Yves

    Computational biology and chemistry

    2019  Volume 79, Page(s) 48–54

    Abstract: A method aiming at investigating possible bioactive conformations of acyl homoserine lactone (AHL) quorum sensing (QS) modulators is established. The method relies on the exhaustive conformational analysis of AHLs by varying torsion angles around the ... ...

    Abstract A method aiming at investigating possible bioactive conformations of acyl homoserine lactone (AHL) quorum sensing (QS) modulators is established. The method relies on the exhaustive conformational analysis of AHLs by varying torsion angles around the amide group then on the selection of the closest conformation to those known from co-crystallized XRD data of AHL-receptor complexes. These latter are then docked as rigid ligand within the receptor binding site, leading to interactions with binding site residues which are highly consistent as compared with the data arising from XRD studies. The method is first validated using AHLs for which XRD data of their complexes with their cognate receptor are available, then extended to examples for which the binding mode is still unknown. Three compounds were used to validate the method: hexanoyl homoserine lactone (HHL) as an example of autoinducer, 3-oxo-butanoyl homoserine lactone (OBHL), as a representative model of 3-oxo-AHLs, and 4-(4-chlorophenoxy)butanoyl homoserine lactone (CPOBHL) as an example of a QS inhibitor. The conformational analysis of these three compounds to their cognate protein (TraR, SdiA, LasR and CviR) provides the data which enable the next rigid docking step. Further rigid docking of the closest conformations compared to the known bioactive ones within the binding sites allows to recover the expected binding mode with high precision (atomic RMSD < 2 Å). This "conformational analysis/torsion angle filter/rigid ligand docking" method was then used for investigating three non-natural AHL-type QS inhibitors without known co-crystallized XRD structures, namely was 2-hexenoyl homoserine lactone (HenHL), 3-oxo-4-phenylbutanoyl homoserine lactone (OPBHL) and 3-(4-bromophenyl)propanoyl homoserine lactone (BPPHL). Results provide insights into their possible binding mode by identifying specific interactions with some key residues within the receptor binding site, allowing discussion of their biological activity.
    MeSH term(s) 4-Butyrolactone/analogs & derivatives ; 4-Butyrolactone/chemical synthesis ; 4-Butyrolactone/chemistry ; 4-Butyrolactone/pharmacology ; Ligands ; Molecular Conformation ; Molecular Docking Simulation ; Quorum Sensing/drug effects ; Structure-Activity Relationship
    Chemical Substances Ligands ; homoserine lactone (1192-20-7) ; 4-Butyrolactone (OL659KIY4X)
    Language English
    Publishing date 2019-01-19
    Publishing country England
    Document type Journal Article
    ISSN 1476-928X
    ISSN (online) 1476-928X
    DOI 10.1016/j.compbiolchem.2019.01.006
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  8. Article ; Online: Biological Evaluation and Docking Studies of New Carbamate, Thiocarbamate, and Hydrazide Analogues of Acyl Homoserine Lactones as

    Zhang, Qiang / Queneau, Yves / Soulère, Laurent

    Biomolecules

    2020  Volume 10, Issue 3

    Abstract: A series of carbamate, thiocarbamate, and hydrazide analogues of acylhomoserine lactones (AHLs) were synthesized and their ability to ... ...

    Abstract A series of carbamate, thiocarbamate, and hydrazide analogues of acylhomoserine lactones (AHLs) were synthesized and their ability to modulate
    MeSH term(s) Acyl-Butyrolactones/chemistry ; Aliivibrio fischeri/chemistry ; Aliivibrio fischeri/metabolism ; Molecular Docking Simulation ; Quorum Sensing ; Repressor Proteins/chemistry ; Repressor Proteins/metabolism ; Thiocarbamates/chemistry ; Trans-Activators/chemistry ; Trans-Activators/metabolism
    Chemical Substances Acyl-Butyrolactones ; Repressor Proteins ; Thiocarbamates ; Trans-Activators ; LuxR autoinducer binding proteins (115038-68-1)
    Language English
    Publishing date 2020-03-15
    Publishing country Switzerland
    Document type Evaluation Study ; Journal Article ; Research Support, Non-U.S. Gov't
    ZDB-ID 2701262-1
    ISSN 2218-273X ; 2218-273X
    ISSN (online) 2218-273X
    ISSN 2218-273X
    DOI 10.3390/biom10030455
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  9. Article ; Online: (2R)- and (2S)- 2-hydroxy- hexanoyl and octanoyl-l-homoserine lactones: New highly potent Quorum Sensing modulators with opposite activities.

    Zhang, Qiang / Jeanneau, Erwann / Queneau, Yves / Soulère, Laurent

    Bioorganic chemistry

    2020  Volume 104, Page(s) 104307

    Abstract: The synthesis and the QS modulation activity of diastereoisomerically pure 2-hydroxy-N-acyl-l-homoserine lactones (2-OH-AHLs) are unveiled. (2R)- and (2S)- 2-hydroxy-N-hexanoyl-l-homoserine lactone and 2-hydroxy-N-octanoyl-l-homoserine lactone have been ... ...

    Abstract The synthesis and the QS modulation activity of diastereoisomerically pure 2-hydroxy-N-acyl-l-homoserine lactones (2-OH-AHLs) are unveiled. (2R)- and (2S)- 2-hydroxy-N-hexanoyl-l-homoserine lactone and 2-hydroxy-N-octanoyl-l-homoserine lactone have been identified as very potent QS agonists and antagonists on the Vibrio fischeri-quorum sensing system with opposite activities depending on the configuration of the carbon atom with the hydroxyl group. Flexible molecular docking showed that the (2R)-OH configuration in the antagonist isomer induces new hydrogen bonds with Tyr70 and Asp79, two importantly conserved residues in the LuxR protein family, while the (2S)-OH agonist configuration exhibits a binding mode comparable to the natural ligand 3-oxo-hexanoyl-l-homoserine lactone (OHHL). For the analogs with long alkyl chain 3a and 3b and aromatic analogs, all are antagonists with no effect of the configuration at C-2.
    MeSH term(s) 4-Butyrolactone/analogs & derivatives ; 4-Butyrolactone/chemical synthesis ; 4-Butyrolactone/chemistry ; 4-Butyrolactone/pharmacology ; Aliivibrio fischeri/drug effects ; Anti-Bacterial Agents/chemical synthesis ; Anti-Bacterial Agents/chemistry ; Anti-Bacterial Agents/pharmacology ; Dose-Response Relationship, Drug ; Escherichia coli/drug effects ; Microbial Sensitivity Tests ; Models, Molecular ; Molecular Structure ; Quorum Sensing/drug effects ; Stereoisomerism ; Structure-Activity Relationship
    Chemical Substances Anti-Bacterial Agents ; homoserine lactone (1192-20-7) ; 4-Butyrolactone (OL659KIY4X)
    Language English
    Publishing date 2020-09-24
    Publishing country United States
    Document type Journal Article ; Research Support, Non-U.S. Gov't
    ZDB-ID 120080-x
    ISSN 1090-2120 ; 0045-2068
    ISSN (online) 1090-2120
    ISSN 0045-2068
    DOI 10.1016/j.bioorg.2020.104307
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    In stock of ZB MED Cologne/Königswinter

    Zs.A 4207: Show issues Location:
    Je nach Verfügbarkeit (siehe Angabe bei Bestand)
    bis Jg. 1994: Bestellungen von Artikeln über das Online-Bestellformular
    Jg. 1995 - 2021: Lesesall (2.OG)
    ab Jg. 2022: Lesesaal (EG)

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  10. Article ; Online: Structural Variations in the Central Heterocyclic Scaffold of Tripartite 2,6-Difluorobenzamides: Influence on Their Antibacterial Activity against MDR

    Barbier, Thibaut / Badiou, Cédric / Davy, Floriane / Queneau, Yves / Dumitrescu, Oana / Lina, Gérard / Soulère, Laurent

    Molecules (Basel, Switzerland)

    2022  Volume 27, Issue 19

    Abstract: Five series of heterocyclic tripartite 2,6-difluorobenzamides, namely 1,2,3-triazoles, 1,2,4- and 1,3,4-oxadiazoles, analogs of reported model anti-staphylococcal compounds, were prepared. The purpose was to investigate the influence of the nature of the ...

    Abstract Five series of heterocyclic tripartite 2,6-difluorobenzamides, namely 1,2,3-triazoles, 1,2,4- and 1,3,4-oxadiazoles, analogs of reported model anti-staphylococcal compounds, were prepared. The purpose was to investigate the influence of the nature of the heterocyclic central scaffold on the biological activity against three strains of
    MeSH term(s) Anti-Bacterial Agents/chemistry ; Anti-Bacterial Agents/pharmacology ; Benzamides ; Humans ; Methicillin-Resistant Staphylococcus aureus ; Microbial Sensitivity Tests ; Oxadiazoles/chemistry ; Oxadiazoles/pharmacology ; Staphylococcal Infections/microbiology ; Staphylococcus aureus ; Triazoles/pharmacology
    Chemical Substances Anti-Bacterial Agents ; Benzamides ; Oxadiazoles ; Triazoles ; 2,6-difluorobenzamide (SJ2RN214MK)
    Language English
    Publishing date 2022-10-05
    Publishing country Switzerland
    Document type Journal Article
    ZDB-ID 1413402-0
    ISSN 1420-3049 ; 1431-5165 ; 1420-3049
    ISSN (online) 1420-3049
    ISSN 1431-5165 ; 1420-3049
    DOI 10.3390/molecules27196619
    Database MEDical Literature Analysis and Retrieval System OnLINE

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