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The Latest Bioinformatics News

Characterizing septum inhibition in Mycobacterium tuberculosis for novel drug... Related Articles

Characterizing septum inhibition in Mycobacterium tuberculosis for novel drug discovery.

Tuberculosis (Edinb). 2008 May 12;

Authors: Respicio L, Nair PA, Huang Q, Anil B, Tracz S, Truglio JJ, Kisker C, Raleigh DP, Ojima I, Knudson DL, Tonge PJ, Slayden RA

A temperature sensitive mutation in the cell division protein FtsZ was used in combination with transcriptional analysis to identify biomarkers for inhibition of septum formation. Crystallography and modeling revealed that the glycine for aspartate substitution at amino acid 210 was located in helix 8 of the protein, adjacent to the T7 synergy loop. To verify the molecular behavior of FtsZ(D210G), the in vitro activity and structural stability were evaluated as a function of temperature. These analyses confirmed that the FtsZ(D210G) mutant had reduced GTPase and polymerization activity compared to wild-type FtsZ, and CD spectroscopy demonstrated that both FtsZ(D210G) and wild-type FtsZ had similar structure and stability. Significantly, the FtsZ(D210G) merodiploid strain of M. tuberculosis had compromised growth at 37 degrees C, substantiating the suitability of FtsZ(D210G) as a molecular tool for global analysis in response to improper FtsZ polymerization and septum inhibition. Advanced model-based bioinformatics and transcriptional mapping were used to identify high-content multiple features that provide biomarkers for the development of a rational drug screening platform for discovering novel chemotherapeutics that target cell division.

PMID: 18479968 [PubMed - as supplied by publisher]

Exploiting Protein Fluctuations at the Active-Site Gorge of Human Cholinester... Related Articles

Exploiting Protein Fluctuations at the Active-Site Gorge of Human Cholinesterases: Further Optimization of the Design Strategy to Develop Extremely Potent Inhibitors.

J Med Chem. 2008 May 15;

Authors: Butini S, Campiani G, Borriello M, Gemma S, Panico A, Persico M, Catalanotti B, Ros S, Brindisi M, Agnusdei M, Fiorini I, Nacci V, Novellino E, Belinskaya T, Saxena A, Fattorusso C

Protein conformational fluctuations are critical for biological functions, although the relationship between protein motion and function has yet to be fully explored. By a thorough bioinformatics analysis of cholinesterases (ChEs), we identified specific hot spots, responsible for protein fluctuations and functions, and those active-site residues that play a role in modulating the cooperative network among the key substructures. This drew the optimization of our design strategy to discover potent and reversible inhibitors of human acetylcholinesterase and butyrylcholinesterase ( hAChE and hBuChE) that selectively interact with specific protein substructures. Accordingly, two tricyclic moieties differently spaced by functionalized linkers were investigated as molecular yardsticks to probe the finest interactions with specific hot spots in the hChE gorge. A number of SAR trends were identified, and the multisite inhibitors 3a and 3d were found to be the most potent inhibitors of hBuChE and hAChE known to date.

PMID: 18479118 [PubMed - as supplied by publisher]