The Experts below are selected from a list of 75 Experts worldwide ranked by ideXlab platform

Ferrari Erika - One of the best experts on this subject based on the ideXlab platform.

  • Synthesis, characterization and Metal coordination of a potential β-lactamase inhibitor: 5-Methyl-2-phenoxymethyl-3-H-imidazole-4-carboxylic acid (PIMA)
    'Elsevier BV', 2017
    Co-Authors: Romagnoli Chiara, Prati Fabio, Benassi Rois, Orteca Giulia, Saladini Monica, Ferrari Erika
    Abstract:

    Among relevant Metal ions in biological systems, zinc and iron play a key role as active partners of the catalytic machinery. In particular, the inhibition of Metal Enzymes that are involved in physiological and pathological processes has been deeply investigated for the rational design of selective and efficient drugs based on chelators. Since imidazole histidine residue is one of the most versatile sites in proteins, especially in Enzymes acting in the presence of Metal ions as cofactors, in this work the synthesis and characterization of a new imidazole derivative, namely 5-methyl-2-phenoxymethyl-3-H-imidazole-4-carboxylic acid (PIMA) is reported. PIMA was designed as Metallo-\uce\ub2-lactamase inhibitor thanks to its similarity with penicillin V, a \uce\ub2-lactam antibiotic inactivated by Metallo-\uce\ub2-lactamase, for which there are no commercially available inhibitors. The evaluation of PIMA coordinating ability toward iron, zinc, and gallium, these latter selected as a non-paramagnetic probe for iron, is performed by theoretical DFT calculations and in solution by experimental techniques, i.e. potentiometry, UV-vis and NMR spectroscopy. PIMA exhibits an efficient Metal chelating ability; the prevailing species in physiological condition are ML3 for Fe3+ and Ga3+ and ML2 for Zn2+, in which chelation is due to deprotonated carboxylic oxygen and imidazole nitrogen in the N,O donor set. The demonstrated ability of PIMA to chelate zinc ion, combined with its structure similarity with penicillin V, supports further exploration of this imidazole-4-carboxylate as Metallo-\uce\ub2-lactamase inhibitor

  • Synthesis, characterization and Metal coordination of a potential β-lactamase inhibitor: 5-Methyl-2-phenoxymethyl-3-H-imidazole-4-carboxylic acid (PIMA)
    2015
    Co-Authors: Romagnoli Chiara, Prati Fabio, Benassi Rois, Orteca Giulia, Saladini Monica, Ferrari Erika
    Abstract:

    AbstractAmong relevant Metal ions in biological systems, zinc and iron play a key role as active partners of the catalytic machinery. In particular, the inhibition of Metal Enzymes that are involved in physiological and pathological processes has been deeply investigated for the rational design of selective and efficient drugs based on chelators. Since imidazole histidine residue is one of the most versatile sites in proteins, especially in Enzymes acting in the presence of Metal ions as cofactors, in this work the synthesis and characterization of a new imidazole derivative, namely 5-methyl-2-phenoxymethyl-3-H-imidazole-4-carboxylic acid (PIMA) is reported. PIMA was designed as Metallo-β-lactamase inhibitor thanks to its similarity with penicillin V, a β-lactam antibiotic inactivated by Metallo-β-lactamase, for which there are no commercially available inhibitors. The evaluation of PIMA coordinating ability toward iron, zinc, and gallium, these latter selected as a non-paramagnetic probe for iron, is performed by theoretical DFT calculations and in solution by experimental techniques, i.e. potentiometry, UV–vis and NMR spectroscopy. PIMA exhibits an efficient Metal chelating ability; the prevailing species in physiological condition are ML3 for Fe3+ and Ga3+ and ML2 for Zn2+, in which chelation is due to deprotonated carboxylic oxygen and imidazole nitrogen in the N,O donor set. The demonstrated ability of PIMA to chelate zinc ion, combined with its structure similarity with penicillin V, supports further exploration of this imidazole-4-carboxylate as Metallo-β-lactamase inhibitor

Sarvendra Kumar - One of the best experts on this subject based on the ideXlab platform.

  • antimicrobial and sod activities of novel transition Metal complexes of pyridine 2 6 dicarboxylic acid containing 4 picoline as auxiliary ligand
    European Journal of Medicinal Chemistry, 2010
    Co-Authors: Zafar A Siddiqi, Mohd Khalid, Sarvendra Kumar, Mohammad Shahid, Shabana Noor
    Abstract:

    Abstract Ternary complexes are potential models for several mono and polynuclear Metal Enzymes. The present ternary complexes [Fe(dipic)(4-picoline)]Cl, [M(dipic)(4-picoline)] [M = Co or Ni] and [Cu(dipic)(4-picoline)]n were prepared to exploit as novel antimicrobial agents. The chemical structure and bonding etc. were elucidated by spectral studies. Single crystal X-ray data of the Cu(II) complex indicated formation of 1D coordination polymeric structure. The antimicrobial activities investigated against Escherichia coli (K-12), Bacillus subtilis (MTCC-121), Staphylococcus aureus (IOA-SA-22), Salmonella typhymurium (MTCC-98), Candida albicans, Aspergillus fumigatus and Penicillium marneffei (isolates from Department of Microbiology, Faculty of Agricultural Science, AMU) showed significant activities. The superoxide dismutase (SOD) activity of the Cu(II) complex was also assessed by NBT assay.

  • antimicrobial and sod activities of novel transition Metal ternary complexes of iminodiacetic acid containing α diimine as auxiliary ligand
    European Journal of Medicinal Chemistry, 2009
    Co-Authors: Zafar A Siddiqi, Mohd Khalid, Mohammad Shahid, Sarvendra Kumar
    Abstract:

    Abstract Ternary complexes containing an α-diimine auxiliary ligand have been widely used as models for several mono and polynuclear Metal Enzymes. The present ternary complexes [M(IDA)(Phen)H2O]·xH2O (x = 2, 3 or 4) were prepared as novel antimicrobial agents employing reactions of Cu(OAc)2 or MCl2 (M = Co, Ni, Cr) with iminodiacetic acid (H2IDA) in the presence of 1,10-phenanthroline (Phen), whose chemical structure and bonding were elucidated by IR, FAB-Mass, 1H, 13C NMR, EPR spectral and elemental analyses. The antimicrobial activities against Escherichia coli (K-12), Bacillus subtilis (MTCC 121), Staphylococcus aureus (IOA-SA-22), Salmonella typhimurium (MTCC 98), Candida albicans, Aspergillus fumigatus and Penicillium marneffei (isolates from Department of Microbiology, Faculty of Agricultural Science, AMU) were investigated and significant activities were obtained. The superoxide dismutase activity of the Cu(II) complex was assessed by NBT assay. The single crystal X-ray structure for [Cu(IDA)(Phen)H2O]·2H2O indicates a triclinic unit cell in P-1 space group with structural parameters, a = 6.745(5), b = 10.551(5), c = 11.414(5) A, α = 95.770(5), β = 91.396(5), γ = 92.518(5)° and presence of an extensive H-bonding and π–π stacking interactions which generate a supramolecular framework.

Romagnoli Chiara - One of the best experts on this subject based on the ideXlab platform.

  • Synthesis, characterization and Metal coordination of a potential β-lactamase inhibitor: 5-Methyl-2-phenoxymethyl-3-H-imidazole-4-carboxylic acid (PIMA)
    'Elsevier BV', 2017
    Co-Authors: Romagnoli Chiara, Prati Fabio, Benassi Rois, Orteca Giulia, Saladini Monica, Ferrari Erika
    Abstract:

    Among relevant Metal ions in biological systems, zinc and iron play a key role as active partners of the catalytic machinery. In particular, the inhibition of Metal Enzymes that are involved in physiological and pathological processes has been deeply investigated for the rational design of selective and efficient drugs based on chelators. Since imidazole histidine residue is one of the most versatile sites in proteins, especially in Enzymes acting in the presence of Metal ions as cofactors, in this work the synthesis and characterization of a new imidazole derivative, namely 5-methyl-2-phenoxymethyl-3-H-imidazole-4-carboxylic acid (PIMA) is reported. PIMA was designed as Metallo-\uce\ub2-lactamase inhibitor thanks to its similarity with penicillin V, a \uce\ub2-lactam antibiotic inactivated by Metallo-\uce\ub2-lactamase, for which there are no commercially available inhibitors. The evaluation of PIMA coordinating ability toward iron, zinc, and gallium, these latter selected as a non-paramagnetic probe for iron, is performed by theoretical DFT calculations and in solution by experimental techniques, i.e. potentiometry, UV-vis and NMR spectroscopy. PIMA exhibits an efficient Metal chelating ability; the prevailing species in physiological condition are ML3 for Fe3+ and Ga3+ and ML2 for Zn2+, in which chelation is due to deprotonated carboxylic oxygen and imidazole nitrogen in the N,O donor set. The demonstrated ability of PIMA to chelate zinc ion, combined with its structure similarity with penicillin V, supports further exploration of this imidazole-4-carboxylate as Metallo-\uce\ub2-lactamase inhibitor

  • Synthesis, characterization and Metal coordination of a potential β-lactamase inhibitor: 5-Methyl-2-phenoxymethyl-3-H-imidazole-4-carboxylic acid (PIMA)
    2015
    Co-Authors: Romagnoli Chiara, Prati Fabio, Benassi Rois, Orteca Giulia, Saladini Monica, Ferrari Erika
    Abstract:

    AbstractAmong relevant Metal ions in biological systems, zinc and iron play a key role as active partners of the catalytic machinery. In particular, the inhibition of Metal Enzymes that are involved in physiological and pathological processes has been deeply investigated for the rational design of selective and efficient drugs based on chelators. Since imidazole histidine residue is one of the most versatile sites in proteins, especially in Enzymes acting in the presence of Metal ions as cofactors, in this work the synthesis and characterization of a new imidazole derivative, namely 5-methyl-2-phenoxymethyl-3-H-imidazole-4-carboxylic acid (PIMA) is reported. PIMA was designed as Metallo-β-lactamase inhibitor thanks to its similarity with penicillin V, a β-lactam antibiotic inactivated by Metallo-β-lactamase, for which there are no commercially available inhibitors. The evaluation of PIMA coordinating ability toward iron, zinc, and gallium, these latter selected as a non-paramagnetic probe for iron, is performed by theoretical DFT calculations and in solution by experimental techniques, i.e. potentiometry, UV–vis and NMR spectroscopy. PIMA exhibits an efficient Metal chelating ability; the prevailing species in physiological condition are ML3 for Fe3+ and Ga3+ and ML2 for Zn2+, in which chelation is due to deprotonated carboxylic oxygen and imidazole nitrogen in the N,O donor set. The demonstrated ability of PIMA to chelate zinc ion, combined with its structure similarity with penicillin V, supports further exploration of this imidazole-4-carboxylate as Metallo-β-lactamase inhibitor

Zafar A Siddiqi - One of the best experts on this subject based on the ideXlab platform.

  • antimicrobial and sod activities of novel transition Metal complexes of pyridine 2 6 dicarboxylic acid containing 4 picoline as auxiliary ligand
    European Journal of Medicinal Chemistry, 2010
    Co-Authors: Zafar A Siddiqi, Mohd Khalid, Sarvendra Kumar, Mohammad Shahid, Shabana Noor
    Abstract:

    Abstract Ternary complexes are potential models for several mono and polynuclear Metal Enzymes. The present ternary complexes [Fe(dipic)(4-picoline)]Cl, [M(dipic)(4-picoline)] [M = Co or Ni] and [Cu(dipic)(4-picoline)]n were prepared to exploit as novel antimicrobial agents. The chemical structure and bonding etc. were elucidated by spectral studies. Single crystal X-ray data of the Cu(II) complex indicated formation of 1D coordination polymeric structure. The antimicrobial activities investigated against Escherichia coli (K-12), Bacillus subtilis (MTCC-121), Staphylococcus aureus (IOA-SA-22), Salmonella typhymurium (MTCC-98), Candida albicans, Aspergillus fumigatus and Penicillium marneffei (isolates from Department of Microbiology, Faculty of Agricultural Science, AMU) showed significant activities. The superoxide dismutase (SOD) activity of the Cu(II) complex was also assessed by NBT assay.

  • antimicrobial and sod activities of novel transition Metal ternary complexes of iminodiacetic acid containing α diimine as auxiliary ligand
    European Journal of Medicinal Chemistry, 2009
    Co-Authors: Zafar A Siddiqi, Mohd Khalid, Mohammad Shahid, Sarvendra Kumar
    Abstract:

    Abstract Ternary complexes containing an α-diimine auxiliary ligand have been widely used as models for several mono and polynuclear Metal Enzymes. The present ternary complexes [M(IDA)(Phen)H2O]·xH2O (x = 2, 3 or 4) were prepared as novel antimicrobial agents employing reactions of Cu(OAc)2 or MCl2 (M = Co, Ni, Cr) with iminodiacetic acid (H2IDA) in the presence of 1,10-phenanthroline (Phen), whose chemical structure and bonding were elucidated by IR, FAB-Mass, 1H, 13C NMR, EPR spectral and elemental analyses. The antimicrobial activities against Escherichia coli (K-12), Bacillus subtilis (MTCC 121), Staphylococcus aureus (IOA-SA-22), Salmonella typhimurium (MTCC 98), Candida albicans, Aspergillus fumigatus and Penicillium marneffei (isolates from Department of Microbiology, Faculty of Agricultural Science, AMU) were investigated and significant activities were obtained. The superoxide dismutase activity of the Cu(II) complex was assessed by NBT assay. The single crystal X-ray structure for [Cu(IDA)(Phen)H2O]·2H2O indicates a triclinic unit cell in P-1 space group with structural parameters, a = 6.745(5), b = 10.551(5), c = 11.414(5) A, α = 95.770(5), β = 91.396(5), γ = 92.518(5)° and presence of an extensive H-bonding and π–π stacking interactions which generate a supramolecular framework.

Ulrich Ermler - One of the best experts on this subject based on the ideXlab platform.

  • conserving energy with sulfate around 100 c structure and mechanism of key Metal Enzymes in hyperthermophilic archaeoglobus fulgidus
    Metallomics, 2013
    Co-Authors: Günter Fritz, Ulrich Ermler
    Abstract:

    Sulfate-reducing bacteria and archaea are important players in the biogeochemical sulfur cycle. ATP sulfurylase, adenosine 5′-phosphosulfate reductase and dissimilatory sulfite reductase are the key Enzymes in the energy conserving process of SO42− → H2S reduction. This review summarizes recent advances in our understanding of the activation of sulfate to adenosine 5′-phosphosulfate, the following reductive cleavage to SO32− and AMP, and the final six-electron reduction of SO32− to H2S in the hyperthermophilic archaeon Archaeoglobus fulgidus. Structure based mechanisms will be discussed for these three Enzymes which host unique Metal centers at their catalytic sites.

  • active sites of transition Metal Enzymes with a focus on nickel
    Current Opinion in Structural Biology, 1998
    Co-Authors: Ulrich Ermler, Wolfgang Grabarse, Seigo Shima, Marcel Goubeaud, Rudolf K Thauer
    Abstract:

    Since 1995, crystal structures have been determined for many transition-Metal Enzymes, in particular those containing the rarely used transition Metals vanadium, molybdenum, tungsten, manganese, cobalt and nickel. Accordingly, our understanding of how an enzyme uses the unique properties of a specific transition Metal has been substantially increased in the past few years. The different functions of nickel in catalysis are highlighted by describing the active sites of six nickel Enzymes - methyl-coenyzme M reductase, urease, hydrogenase, superoxide dismutase, carbon monoxide dehydrogenase and acetyl-coenzyme A synthase.