Research Topics
| Sergio C ChaiSummaryAffiliation: Indiana University Country: USA Publications
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Publications
Analysis of the stoichiometric metal activation of methionine aminopeptidaseSergio C Chai
Department of Biochemistry and Molecular Biology, Indiana University School of Medicine, Indianapolis, Indiana 46202, USA
BMC Biochem 10:32. 2009..Herein, we report a mathematical model and detailed analysis of the stoichiometric activation of MetAP by metal cofactors...- Catalysis and inhibition of Mycobacterium tuberculosis methionine aminopeptidaseJing Ping Lu
Department of Biochemistry and Molecular Biology, Indiana University School of Medicine, 635 Barnhill Drive, Indianapolis, Indiana 46202, USA
J Med Chem 53:1329-37. 2010..Finally, X-ray structures of MtMetAP1c in complex with three metalloform-selective inhibitors were analyzed, which showed different binding modes and different interactions with metal ions and active site residues... - Discovery of inhibitors of Escherichia coli methionine aminopeptidase with the Fe(II)-form selectivity and antibacterial activityWen Long Wang
Department of Biochemistry and Molecular Biology, Indiana University School of Medicine, Indianapolis, Indiana 46202, USA
J Med Chem 51:6110-20. 2008..Our data indicate that Fe(II) is the likely metal used by MetAP in the cellular environment, and MetAP inhibitors need to inhibit this metalloform of MetAP effectively to be therapeutically useful... - Synthesis and structure-function analysis of Fe(II)-form-selective antibacterial inhibitors of Escherichia coli methionine aminopeptidaseWen Long Wang
Department of Biochemistry and Molecular Biology, Indiana University School of Medicine, 635 Barnhill Drive, Indianapolis, IN 46202, USA
Bioorg Med Chem Lett 19:1080-3. 2009..coli AS19 strain. These findings provide useful information for the design and discovery of more effective MetAP inhibitors for therapeutic applications... - Metal-mediated inhibition is a viable approach for inhibiting cellular methionine aminopeptidaseSergio C Chai
Department of Biochemistry and Molecular Biology, Indiana University School of Medicine, Indianapolis, IN 46202, USA
Bioorg Med Chem Lett 19:6862-4. 2009..Contrary to previous beliefs, this shows that metal-mediated inhibition is a viable approach for discovering MetAP inhibitors that are effective for therapeutic application... - Synthesis and biological evaluation of salicylate-based compounds as a novel class of methionine aminopeptidase inhibitorsWen Long Wang
Department of Biochemistry and Molecular Biology, Indiana University School of Medicine, Indianapolis, IN 46202, USA
Bioorg Med Chem Lett 21:7151-4. 2011..These findings are consistent with our previous conclusion that Fe(II) is the likely metal used by MetAP in bacterial cells and provide new lead structures that can be further developed as novel antibacterial agents... - Determination of binding affinity of metal cofactor to the active site of methionine aminopeptidase based on quantitation of functional enzymeSergio C Chai
Department of Biochemistry and Molecular Biology, Indiana University School of Medicine, Indianapolis, IN 46202, USA
Anal Biochem 395:263-4. 2009..We applied this concept to methionine aminopeptidase from Mycobacterium tuberculosis and showed that it is a monometalated enzyme with a K(D) of 0.13 microM for Co(2+)... - Growth inhibition of Escherichia coli and methicillin-resistant Staphylococcus aureus by targeting cellular methionine aminopeptidaseSergio C Chai
Department of Biochemistry and Molecular Biology, Indiana University School of Medicine, 635 Barnhill Drive, Indianapolis, IN 46202, USA
Eur J Med Chem 46:3537-40. 2011..coli cells. These findings can serve as foundation for the development of novel therapeutics against an ever increasing threat by drug resistant staphylococcal infections... - A cell-based assay that targets methionine aminopeptidase in a physiologically relevant environmentSergio C Chai
Department of Biochemistry and Molecular Biology, Indiana University School of Medicine, Indianapolis, IN 46202, USA
Bioorg Med Chem Lett 20:2129-32. 2010..This cell-based assay is applicable to those cellular targets with poorly defined native cofactor, increasing the chances of identifying inhibitors that can inhibit the cellular target... - Hydrophilic residues are crucial for ribosomal protein L11 (RPL11) interaction with zinc finger domain of MDM2 and p53 protein activationQi Zhang
Department of Biochemistry and Molecular Biology, Indiana University School of Medicine Simon Cancer Center, Indianapolis, Indiana 46032, USA
J Biol Chem 286:38264-74. 2011.... - Two methionine aminopeptidases from Acinetobacter baumannii are functional enzymesHai Yuan
Department of Biochemistry and Molecular Biology, Indiana University School of Medicine, Indianapolis, IN 46202, USA
Bioorg Med Chem Lett 21:3395-8. 2011..The similarity of their catalysis and inhibition to other MetAP enzymes confirmed that both may function as competent MetAP enzymes in A. baumannii and either or both may serve as the potential drug target... - Novel pyrrolopyrimidine-based α-helix mimetics: cell-permeable inhibitors of protein−protein interactionsJi Hoon Lee
Department of Biochemistry and Molecular Biology, and Indiana University Simon Cancer Center, Indiana University School of Medicine, Indianapolis, Indiana 46202, United States
J Am Chem Soc 133:676-9. 2011..Using a fluorescence polarization-based assay, we identified cell-permeable, dual MDMX/MDM2 inhibitors, demonstrating that the designed molecules can act as α-helix mimetics... - FE(II) is the native cofactor for Escherichia coli methionine aminopeptidaseSergio C Chai
Department of Biochemistry and Molecular Biology, Indiana University School of Medicine, Indianapolis, Indiana 46202, USA
J Biol Chem 283:26879-85. 2008..Therefore, we conclude that Fe(II) is the likely metal used by MetAP in E. coli and other bacterial cells...