Peptide deformylase inhibitors of Mycobacterium tuberculosis: Synthesis, structural investigations, and biological results
Bacterial peptide deformylase (PDF) belongs to a subfamily of metalloproteases catalyzing the removal of the N-terminal formyl group from newly synthesized proteins. We report the synthesis and biological activity of highly potent inhibitors of Mycobacterium tuberculosis ( Mtb) PDF enzyme as well as...
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| Veröffentlicht in: | Bioorganic & medicinal chemistry 2008-12, Vol.18 (24), p.6568-6572 |
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| creator | Pichota, Arkadius Duraiswamy, Jeyaraj Yin, Zheng Keller, Thomas H. Alam, Jenefer Liung, Sarah Lee, Gladys Ding, Mei Wang, Gang Chan, Wai Ling Schreiber, Mark Ma, Ida Beer, David Ngew, Xinyi Mukherjee, Kakoli Nanjundappa, Mahesh Teo, Jeanette W.P. Thayalan, Pamela Yap, Amelia Dick, Thomas Meng, Wuyi Xu, Mei Koehn, James Pan, Shi-Hao Clark, Kirk Xie, Xiaoling Shoen, Carolyn Cynamon, Michael |
| description | Bacterial peptide deformylase (PDF) belongs to a subfamily of metalloproteases catalyzing the removal of the N-terminal formyl group from newly synthesized proteins. We report the synthesis and biological activity of highly potent inhibitors of
Mycobacterium tuberculosis (
Mtb) PDF enzyme as well as the first X-ray crystal structure of Mtb PDF. Structure–activity relationship and crystallographic data clarified the structural requirements for high enzyme potency and cell based potency. Activities against single and multi-drug-resistant Mtb strains are also reported. |
| doi_str_mv | 10.1016/j.bmcl.2008.10.040 |
| format | Article |
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Mycobacterium tuberculosis (
Mtb) PDF enzyme as well as the first X-ray crystal structure of Mtb PDF. Structure–activity relationship and crystallographic data clarified the structural requirements for high enzyme potency and cell based potency. Activities against single and multi-drug-resistant Mtb strains are also reported.</description><identifier>ISSN: 0960-894X</identifier><identifier>ISSN: 0968-0896</identifier><identifier>EISSN: 1464-3405</identifier><identifier>EISSN: 1464-3391</identifier><identifier>DOI: 10.1016/j.bmcl.2008.10.040</identifier><identifier>PMID: 19008098</identifier><language>eng</language><publisher>Amsterdam: Elsevier Ltd</publisher><subject>Amidohydrolases - antagonists & inhibitors ; Amidohydrolases - chemistry ; Antibacterial ; Antibacterial agents ; Antibiotics. Antiinfectious agents. Antiparasitic agents ; Antitubercular Agents - chemistry ; Antitubercular Agents - therapeutic use ; Biological and medical sciences ; Chemistry, Pharmaceutical - methods ; Crystallography, X-Ray - methods ; Drug Design ; Drug Resistance, Multiple ; Fluoroquinolones - pharmacology ; Humans ; Inhibitory Concentration 50 ; Medical sciences ; Microbial Sensitivity Tests ; Models, Chemical ; Molecular Conformation ; Mycobacterium bovis - metabolism ; Mycobacterium tuberculosis ; Mycobacterium tuberculosis - drug effects ; Mycobacterium tuberculosis - metabolism ; PDF ; Pharmacology. Drug treatments ; SAR ; Tuberculosis - drug therapy ; X-Ray</subject><ispartof>Bioorganic & medicinal chemistry, 2008-12, Vol.18 (24), p.6568-6572</ispartof><rights>2008 Elsevier Ltd</rights><rights>2009 INIST-CNRS</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c415t-8167395815bd49607b58e09e008f498f59fa307a1ec86bca5e9340d91b1c681d3</citedby><cites>FETCH-LOGICAL-c415t-8167395815bd49607b58e09e008f498f59fa307a1ec86bca5e9340d91b1c681d3</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktohtml>$$Uhttps://dx.doi.org/10.1016/j.bmcl.2008.10.040$$EHTML$$P50$$Gelsevier$$H</linktohtml><link.rule.ids>315,782,786,3552,27931,27932,46002</link.rule.ids><backlink>$$Uhttp://pascal-francis.inist.fr/vibad/index.php?action=getRecordDetail&idt=20919057$$DView record in Pascal Francis$$Hfree_for_read</backlink><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/19008098$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Pichota, Arkadius</creatorcontrib><creatorcontrib>Duraiswamy, Jeyaraj</creatorcontrib><creatorcontrib>Yin, Zheng</creatorcontrib><creatorcontrib>Keller, Thomas H.</creatorcontrib><creatorcontrib>Alam, Jenefer</creatorcontrib><creatorcontrib>Liung, Sarah</creatorcontrib><creatorcontrib>Lee, Gladys</creatorcontrib><creatorcontrib>Ding, Mei</creatorcontrib><creatorcontrib>Wang, Gang</creatorcontrib><creatorcontrib>Chan, Wai Ling</creatorcontrib><creatorcontrib>Schreiber, Mark</creatorcontrib><creatorcontrib>Ma, Ida</creatorcontrib><creatorcontrib>Beer, David</creatorcontrib><creatorcontrib>Ngew, Xinyi</creatorcontrib><creatorcontrib>Mukherjee, Kakoli</creatorcontrib><creatorcontrib>Nanjundappa, Mahesh</creatorcontrib><creatorcontrib>Teo, Jeanette W.P.</creatorcontrib><creatorcontrib>Thayalan, Pamela</creatorcontrib><creatorcontrib>Yap, Amelia</creatorcontrib><creatorcontrib>Dick, Thomas</creatorcontrib><creatorcontrib>Meng, Wuyi</creatorcontrib><creatorcontrib>Xu, Mei</creatorcontrib><creatorcontrib>Koehn, James</creatorcontrib><creatorcontrib>Pan, Shi-Hao</creatorcontrib><creatorcontrib>Clark, Kirk</creatorcontrib><creatorcontrib>Xie, Xiaoling</creatorcontrib><creatorcontrib>Shoen, Carolyn</creatorcontrib><creatorcontrib>Cynamon, Michael</creatorcontrib><title>Peptide deformylase inhibitors of Mycobacterium tuberculosis: Synthesis, structural investigations, and biological results</title><title>Bioorganic & medicinal chemistry</title><addtitle>Bioorg Med Chem Lett</addtitle><description>Bacterial peptide deformylase (PDF) belongs to a subfamily of metalloproteases catalyzing the removal of the N-terminal formyl group from newly synthesized proteins. We report the synthesis and biological activity of highly potent inhibitors of
Mycobacterium tuberculosis (
Mtb) PDF enzyme as well as the first X-ray crystal structure of Mtb PDF. Structure–activity relationship and crystallographic data clarified the structural requirements for high enzyme potency and cell based potency. Activities against single and multi-drug-resistant Mtb strains are also reported.</description><subject>Amidohydrolases - antagonists & inhibitors</subject><subject>Amidohydrolases - chemistry</subject><subject>Antibacterial</subject><subject>Antibacterial agents</subject><subject>Antibiotics. Antiinfectious agents. Antiparasitic agents</subject><subject>Antitubercular Agents - chemistry</subject><subject>Antitubercular Agents - therapeutic use</subject><subject>Biological and medical sciences</subject><subject>Chemistry, Pharmaceutical - methods</subject><subject>Crystallography, X-Ray - methods</subject><subject>Drug Design</subject><subject>Drug Resistance, Multiple</subject><subject>Fluoroquinolones - pharmacology</subject><subject>Humans</subject><subject>Inhibitory Concentration 50</subject><subject>Medical sciences</subject><subject>Microbial Sensitivity Tests</subject><subject>Models, Chemical</subject><subject>Molecular Conformation</subject><subject>Mycobacterium bovis - metabolism</subject><subject>Mycobacterium tuberculosis</subject><subject>Mycobacterium tuberculosis - drug effects</subject><subject>Mycobacterium tuberculosis - metabolism</subject><subject>PDF</subject><subject>Pharmacology. Drug treatments</subject><subject>SAR</subject><subject>Tuberculosis - drug therapy</subject><subject>X-Ray</subject><issn>0960-894X</issn><issn>0968-0896</issn><issn>1464-3405</issn><issn>1464-3391</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2008</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNp9kE1vEzEQhi0EoqHwBzigvcCJTe3EdtaIC6r4klqBBEjcLH_Mto686-CxK4Vfj6NE9NbTjGaedzTvS8hLRpeMMnmxXdrJxeWK0qENlpTTR2TBuOT9mlPxmCyokrQfFP99Rp4hbillnHL-lJwx1TRUDQvy9zvsSvDQeRhTnvbRIHRhvg02lJSxS2N3vXfJGlcghzp1pVrIrsaEAd91P_ZzuYXWvu2w5OpKzSY2_R1gCTemhDS3lZl9Z0OK6Sa4ts6ANRZ8Tp6MJiK8ONVz8uvTx5-XX_qrb5-_Xn646h1novQDk5u1EgMT1vNmaGPFAFRBczByNYxCjWZNN4aBG6R1RoBq9r1iljk5ML8-J2-Od3c5_antMT0FdBCjmSFV1ExJybiQDVwdQZcTYoZR73KYTN5rRvUhcb3Vh8T1IfHDrCXeRK9O16udwN9LThE34PUJMNjcj9nMLuB_bkVVQ8Wmce-PHLQs7gJkjS7A7MCHDK5on8JDf_wDi--hzA</recordid><startdate>20081215</startdate><enddate>20081215</enddate><creator>Pichota, Arkadius</creator><creator>Duraiswamy, Jeyaraj</creator><creator>Yin, Zheng</creator><creator>Keller, Thomas H.</creator><creator>Alam, Jenefer</creator><creator>Liung, Sarah</creator><creator>Lee, Gladys</creator><creator>Ding, Mei</creator><creator>Wang, Gang</creator><creator>Chan, Wai Ling</creator><creator>Schreiber, Mark</creator><creator>Ma, Ida</creator><creator>Beer, David</creator><creator>Ngew, Xinyi</creator><creator>Mukherjee, Kakoli</creator><creator>Nanjundappa, Mahesh</creator><creator>Teo, Jeanette W.P.</creator><creator>Thayalan, Pamela</creator><creator>Yap, Amelia</creator><creator>Dick, Thomas</creator><creator>Meng, Wuyi</creator><creator>Xu, Mei</creator><creator>Koehn, James</creator><creator>Pan, Shi-Hao</creator><creator>Clark, Kirk</creator><creator>Xie, Xiaoling</creator><creator>Shoen, Carolyn</creator><creator>Cynamon, Michael</creator><general>Elsevier Ltd</general><general>Elsevier</general><scope>IQODW</scope><scope>CGR</scope><scope>CUY</scope><scope>CVF</scope><scope>ECM</scope><scope>EIF</scope><scope>NPM</scope><scope>AAYXX</scope><scope>CITATION</scope><scope>7QL</scope><scope>7QO</scope><scope>7T7</scope><scope>8FD</scope><scope>C1K</scope><scope>FR3</scope><scope>P64</scope></search><sort><creationdate>20081215</creationdate><title>Peptide deformylase inhibitors of Mycobacterium tuberculosis: Synthesis, structural investigations, and biological results</title><author>Pichota, Arkadius ; Duraiswamy, Jeyaraj ; Yin, Zheng ; Keller, Thomas H. ; Alam, Jenefer ; Liung, Sarah ; Lee, Gladys ; Ding, Mei ; Wang, Gang ; Chan, Wai Ling ; Schreiber, Mark ; Ma, Ida ; Beer, David ; Ngew, Xinyi ; Mukherjee, Kakoli ; Nanjundappa, Mahesh ; Teo, Jeanette W.P. ; Thayalan, Pamela ; Yap, Amelia ; Dick, Thomas ; Meng, Wuyi ; Xu, Mei ; Koehn, James ; Pan, Shi-Hao ; Clark, Kirk ; Xie, Xiaoling ; Shoen, Carolyn ; Cynamon, Michael</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c415t-8167395815bd49607b58e09e008f498f59fa307a1ec86bca5e9340d91b1c681d3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2008</creationdate><topic>Amidohydrolases - antagonists & inhibitors</topic><topic>Amidohydrolases - chemistry</topic><topic>Antibacterial</topic><topic>Antibacterial agents</topic><topic>Antibiotics. Antiinfectious agents. Antiparasitic agents</topic><topic>Antitubercular Agents - chemistry</topic><topic>Antitubercular Agents - therapeutic use</topic><topic>Biological and medical sciences</topic><topic>Chemistry, Pharmaceutical - methods</topic><topic>Crystallography, X-Ray - methods</topic><topic>Drug Design</topic><topic>Drug Resistance, Multiple</topic><topic>Fluoroquinolones - pharmacology</topic><topic>Humans</topic><topic>Inhibitory Concentration 50</topic><topic>Medical sciences</topic><topic>Microbial Sensitivity Tests</topic><topic>Models, Chemical</topic><topic>Molecular Conformation</topic><topic>Mycobacterium bovis - metabolism</topic><topic>Mycobacterium tuberculosis</topic><topic>Mycobacterium tuberculosis - drug effects</topic><topic>Mycobacterium tuberculosis - metabolism</topic><topic>PDF</topic><topic>Pharmacology. 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We report the synthesis and biological activity of highly potent inhibitors of
Mycobacterium tuberculosis (
Mtb) PDF enzyme as well as the first X-ray crystal structure of Mtb PDF. Structure–activity relationship and crystallographic data clarified the structural requirements for high enzyme potency and cell based potency. Activities against single and multi-drug-resistant Mtb strains are also reported.</abstract><cop>Amsterdam</cop><pub>Elsevier Ltd</pub><pmid>19008098</pmid><doi>10.1016/j.bmcl.2008.10.040</doi><tpages>5</tpages></addata></record> |
| fulltext | fulltext |
| identifier | ISSN: 0960-894X |
| ispartof | Bioorganic & medicinal chemistry, 2008-12, Vol.18 (24), p.6568-6572 |
| issn | 0960-894X 0968-0896 1464-3405 1464-3391 |
| language | eng |
| recordid | cdi_proquest_miscellaneous_19661456 |
| source | MEDLINE; ScienceDirect Journals (5 years ago - present) |
| subjects | Amidohydrolases - antagonists & inhibitors Amidohydrolases - chemistry Antibacterial Antibacterial agents Antibiotics. Antiinfectious agents. Antiparasitic agents Antitubercular Agents - chemistry Antitubercular Agents - therapeutic use Biological and medical sciences Chemistry, Pharmaceutical - methods Crystallography, X-Ray - methods Drug Design Drug Resistance, Multiple Fluoroquinolones - pharmacology Humans Inhibitory Concentration 50 Medical sciences Microbial Sensitivity Tests Models, Chemical Molecular Conformation Mycobacterium bovis - metabolism Mycobacterium tuberculosis Mycobacterium tuberculosis - drug effects Mycobacterium tuberculosis - metabolism Pharmacology. Drug treatments SAR Tuberculosis - drug therapy X-Ray |
| title | Peptide deformylase inhibitors of Mycobacterium tuberculosis: Synthesis, structural investigations, and biological results |
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