The Experts below are selected from a list of 180024 Experts worldwide ranked by ideXlab platform

Vicky M Avery - One of the best experts on this subject based on the ideXlab platform.

Courtney C Aldrich - One of the best experts on this subject based on the ideXlab platform.

  • structure based optimization of pyridoxal 5 phosphate dependent transaminase enzyme bioa inhibitors that target biotin biosynthesis in mycobacterium tuberculosis
    Journal of Medicinal Chemistry, 2017
    Co-Authors: Feng Liu, Surendra Dawadi, Kimberly M Maize, Ran Dai, Sae Woong Park, Dirk Schnappinger, Barry C Finzel, Courtney C Aldrich
    Abstract:

    The pyridoxal 5′-phosphate (PLP)-dependent transaminase BioA catalyzes the second step in the biosynthesis of biotin in Mycobacterium tuberculosis (Mtb) and is an essential enzyme for bacterial survival and persistence in vivo. A promising BioA inhibitor 6 containing an N-aryl, N′-benzoylpiperazine scaffold was previously identified by target-based whole-Cell Screening. Here, we explore the structure–activity relationships (SAR) through the design, synthesis, and biological evaluation of a systematic series of analogues of the original hit using a structure-based drug design strategy, which was enabled by cocrystallization of several analogues with BioA. To confirm target engagement and discern analogues with off-target activity, each compound was evaluated against wild-type (WT) Mtb in biotin-free and -containing medium as well as BioA under- and overexpressing Mtb strains. Conformationally constrained derivative 36 emerged as the most potent analogue with a KD of 76 nM against BioA and a minimum inhibit...

  • Structure-Based Optimization of Pyridoxal 5′-Phosphate-Dependent Transaminase Enzyme (BioA) Inhibitors that Target Biotin Biosynthesis in Mycobacterium tuberculosis
    2017
    Co-Authors: Feng Liu, Surendra Dawadi, Kimberly M Maize, Ran Dai, Sae Woong Park, Dirk Schnappinger, Barry C Finzel, Courtney C Aldrich
    Abstract:

    The pyridoxal 5′-phosphate (PLP)-dependent transaminase BioA catalyzes the second step in the biosynthesis of biotin in Mycobacterium tuberculosis (Mtb) and is an essential enzyme for bacterial survival and persistence in vivo. A promising BioA inhibitor 6 containing an N-aryl, N′-benzoylpiperazine scaffold was previously identified by target-based whole-Cell Screening. Here, we explore the structure–activity relationships (SAR) through the design, synthesis, and biological evaluation of a systematic series of analogues of the original hit using a structure-based drug design strategy, which was enabled by cocrystallization of several analogues with BioA. To confirm target engagement and discern analogues with off-target activity, each compound was evaluated against wild-type (WT) Mtb in biotin-free and -containing medium as well as BioA under- and overexpressing Mtb strains. Conformationally constrained derivative 36 emerged as the most potent analogue with a KD of 76 nM against BioA and a minimum inhibitory concentration of 1.7 μM (0.6 μg/mL) against Mtb in biotin-free medium

Melissa Sykes - One of the best experts on this subject based on the ideXlab platform.

M P Rubtsova - One of the best experts on this subject based on the ideXlab platform.

  • microfluidic droplet platform for ultrahigh throughput single Cell Screening of biodiversity
    Proceedings of the National Academy of Sciences of the United States of America, 2017
    Co-Authors: S S Terekhov, I V Smirnov, A V Stepanova, T V Bobik, Yuliana A Mokrushina, Natalia A Ponomarenko, A A Belogurov, M P Rubtsova
    Abstract:

    Ultrahigh-throughput Screening (uHTS) techniques can identify unique functionality from millions of variants. To mimic the natural selection mechanisms that occur by compartmentalization in vivo, we developed a technique based on single-Cell encapsulation in droplets of a monodisperse microfluidic double water-in-oil-in-water emulsion (MDE). Biocompatible MDE enables in-droplet cultivation of different living species. The combination of droplet-generating machinery with FACS followed by next-generation sequencing and liquid chromatography-mass spectrometry analysis of the secretomes of encapsulated organisms yielded detailed genotype/phenotype descriptions. This platform was probed with uHTS for biocatalysts anchored to yeast with enrichment close to the theoretically calculated limit and Cell-to-Cell interactions. MDE-FACS allowed the identification of human butyrylcholinesterase mutants that undergo self-reactivation after inhibition by the organophosphorus agent paraoxon. The versatility of the platform allowed the identification of bacteria, including slow-growing oral microbiota species that suppress the growth of a common pathogen, Staphylococcus aureus, and predicted which genera were associated with inhibitory activity.

Feng Liu - One of the best experts on this subject based on the ideXlab platform.

  • structure based optimization of pyridoxal 5 phosphate dependent transaminase enzyme bioa inhibitors that target biotin biosynthesis in mycobacterium tuberculosis
    Journal of Medicinal Chemistry, 2017
    Co-Authors: Feng Liu, Surendra Dawadi, Kimberly M Maize, Ran Dai, Sae Woong Park, Dirk Schnappinger, Barry C Finzel, Courtney C Aldrich
    Abstract:

    The pyridoxal 5′-phosphate (PLP)-dependent transaminase BioA catalyzes the second step in the biosynthesis of biotin in Mycobacterium tuberculosis (Mtb) and is an essential enzyme for bacterial survival and persistence in vivo. A promising BioA inhibitor 6 containing an N-aryl, N′-benzoylpiperazine scaffold was previously identified by target-based whole-Cell Screening. Here, we explore the structure–activity relationships (SAR) through the design, synthesis, and biological evaluation of a systematic series of analogues of the original hit using a structure-based drug design strategy, which was enabled by cocrystallization of several analogues with BioA. To confirm target engagement and discern analogues with off-target activity, each compound was evaluated against wild-type (WT) Mtb in biotin-free and -containing medium as well as BioA under- and overexpressing Mtb strains. Conformationally constrained derivative 36 emerged as the most potent analogue with a KD of 76 nM against BioA and a minimum inhibit...

  • Structure-Based Optimization of Pyridoxal 5′-Phosphate-Dependent Transaminase Enzyme (BioA) Inhibitors that Target Biotin Biosynthesis in Mycobacterium tuberculosis
    2017
    Co-Authors: Feng Liu, Surendra Dawadi, Kimberly M Maize, Ran Dai, Sae Woong Park, Dirk Schnappinger, Barry C Finzel, Courtney C Aldrich
    Abstract:

    The pyridoxal 5′-phosphate (PLP)-dependent transaminase BioA catalyzes the second step in the biosynthesis of biotin in Mycobacterium tuberculosis (Mtb) and is an essential enzyme for bacterial survival and persistence in vivo. A promising BioA inhibitor 6 containing an N-aryl, N′-benzoylpiperazine scaffold was previously identified by target-based whole-Cell Screening. Here, we explore the structure–activity relationships (SAR) through the design, synthesis, and biological evaluation of a systematic series of analogues of the original hit using a structure-based drug design strategy, which was enabled by cocrystallization of several analogues with BioA. To confirm target engagement and discern analogues with off-target activity, each compound was evaluated against wild-type (WT) Mtb in biotin-free and -containing medium as well as BioA under- and overexpressing Mtb strains. Conformationally constrained derivative 36 emerged as the most potent analogue with a KD of 76 nM against BioA and a minimum inhibitory concentration of 1.7 μM (0.6 μg/mL) against Mtb in biotin-free medium