Seco-prolinenitrile inhibitors of dipeptidyl peptidase IV define minimal pharmacophore requirements at P1
The synthesis and dipeptidyl peptidase IV inhibitory activity of glycine- and alaninenitrile dipeptides are reported. A series of seco-prolinenitrile-containing dipeptides were synthesized and assayed as inhibitors of the N-terminal sequence-specific serine protease dipeptidyl peptidase IV, a promis...
Gespeichert in:
| Veröffentlicht in: | Bioorganic & medicinal chemistry letters 2006-03, Vol.16 (6), p.1731-1734 |
|---|---|
| Hauptverfasser: | , , , , , , |
| Format: | Artikel |
| Sprache: | eng |
| Schlagworte: | |
| Online-Zugang: | Volltext |
| Tags: |
Tag hinzufügen
Keine Tags, Fügen Sie den ersten Tag hinzu!
|
| container_end_page | 1734 |
|---|---|
| container_issue | 6 |
| container_start_page | 1731 |
| container_title | Bioorganic & medicinal chemistry letters |
| container_volume | 16 |
| creator | Magnin, David R. Taunk, Prakash C. Robertson, James G. Wang, Aiying Marcinkeviciene, Jovita Kirby, Mark S. Hamann, Lawrence G. |
| description | The synthesis and dipeptidyl peptidase IV inhibitory activity of glycine- and alaninenitrile dipeptides are reported.
A series of seco-prolinenitrile-containing dipeptides were synthesized and assayed as inhibitors of the N-terminal sequence-specific serine protease dipeptidyl peptidase IV, a promising new target for treatment of type 2 diabetes. The inhibitors described herein assess the minimum structural requirements at P1 for this enzyme, resulting in the identification of inhibitors with low nM potency. |
| doi_str_mv | 10.1016/j.bmcl.2005.11.098 |
| format | Article |
| fullrecord | <record><control><sourceid>proquest_cross</sourceid><recordid>TN_cdi_proquest_miscellaneous_67636908</recordid><sourceformat>XML</sourceformat><sourcesystem>PC</sourcesystem><els_id>S0960894X05015349</els_id><sourcerecordid>67636908</sourcerecordid><originalsourceid>FETCH-LOGICAL-c415t-69928717d2f48eb40fa88d2f7765bcb7462a1de13fe3ea3fca0612a4e1f2bfe3</originalsourceid><addsrcrecordid>eNqFkU9r3DAQxUVpSTZpvkAPRZfmZldjy5IMvYSQfxBIISH0JmR5xGqxLUfyBvLtq2UXcktOGml-b9C8R8gPYCUwEL83ZTfaoawYa0qAkrXqC1kBF7yoOWu-khVrBStUy_8dk5OUNowBZ5wfkWMQtRRMyhXxj2hDMccw-Aknv0Q_IPXT2nd-CTHR4GjvZ5wX378NdF-YhPTumfbosoaOfvKjyb21iaOxYV6HiDTiy9ZHHHFaEjUL_QvfyTdnhoRnh_OUPF1fPV3eFvcPN3eXF_eF5dAshWjbSkmQfeW4wo4zZ5TKFylF09lOclEZ6BFqhzWa2lnDBFSGI7iqy2-n5Hw_Nu_0ssW06NEni8NgJgzbpIUUtWiZ-hQEyRTUbZ3Bag_aGFKK6PQc88bxTQPTuyD0Ru-C0LsgNIDOQWTRz8P0bTdi_y45OJ-BXwfAJGsGF81kfXrnZNMIJXnm_uw5zJ69eow6WY-TxT7baxfdB__RP_4D9Jyo0w</addsrcrecordid><sourcetype>Aggregation Database</sourcetype><iscdi>true</iscdi><recordtype>article</recordtype><pqid>17081393</pqid></control><display><type>article</type><title>Seco-prolinenitrile inhibitors of dipeptidyl peptidase IV define minimal pharmacophore requirements at P1</title><source>MEDLINE</source><source>Elsevier ScienceDirect Journals Complete</source><creator>Magnin, David R. ; Taunk, Prakash C. ; Robertson, James G. ; Wang, Aiying ; Marcinkeviciene, Jovita ; Kirby, Mark S. ; Hamann, Lawrence G.</creator><creatorcontrib>Magnin, David R. ; Taunk, Prakash C. ; Robertson, James G. ; Wang, Aiying ; Marcinkeviciene, Jovita ; Kirby, Mark S. ; Hamann, Lawrence G.</creatorcontrib><description>The synthesis and dipeptidyl peptidase IV inhibitory activity of glycine- and alaninenitrile dipeptides are reported.
A series of seco-prolinenitrile-containing dipeptides were synthesized and assayed as inhibitors of the N-terminal sequence-specific serine protease dipeptidyl peptidase IV, a promising new target for treatment of type 2 diabetes. The inhibitors described herein assess the minimum structural requirements at P1 for this enzyme, resulting in the identification of inhibitors with low nM potency.</description><identifier>ISSN: 0960-894X</identifier><identifier>EISSN: 1464-3405</identifier><identifier>DOI: 10.1016/j.bmcl.2005.11.098</identifier><identifier>PMID: 16376077</identifier><language>eng</language><publisher>Oxford: Elsevier Ltd</publisher><subject>Adenosine Deaminase - chemistry ; Aniline Compounds - metabolism ; Antidiabetic ; Biological and medical sciences ; Dipeptides - chemical synthesis ; Dipeptides - chemistry ; Dipeptides - pharmacology ; Dipeptidyl Peptidase 4 - chemistry ; Dipeptidyl peptidase IV ; Enzyme inhibitors ; Enzyme Inhibitors - chemical synthesis ; Enzyme Inhibitors - chemistry ; Enzyme Inhibitors - pharmacology ; General and cellular metabolism. Vitamins ; Glycoproteins - chemistry ; Humans ; Medical sciences ; Nitriles - chemical synthesis ; Nitriles - chemistry ; Nitriles - pharmacology ; Pharmacology. Drug treatments ; Proline - chemistry ; Serine protease</subject><ispartof>Bioorganic & medicinal chemistry letters, 2006-03, Vol.16 (6), p.1731-1734</ispartof><rights>2005 Elsevier Ltd</rights><rights>2006 INIST-CNRS</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c415t-69928717d2f48eb40fa88d2f7765bcb7462a1de13fe3ea3fca0612a4e1f2bfe3</citedby><cites>FETCH-LOGICAL-c415t-69928717d2f48eb40fa88d2f7765bcb7462a1de13fe3ea3fca0612a4e1f2bfe3</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.2005.11.098$$EHTML$$P50$$Gelsevier$$H</linktohtml><link.rule.ids>315,781,785,3551,27929,27930,46000</link.rule.ids><backlink>$$Uhttp://pascal-francis.inist.fr/vibad/index.php?action=getRecordDetail&idt=17556874$$DView record in Pascal Francis$$Hfree_for_read</backlink><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/16376077$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Magnin, David R.</creatorcontrib><creatorcontrib>Taunk, Prakash C.</creatorcontrib><creatorcontrib>Robertson, James G.</creatorcontrib><creatorcontrib>Wang, Aiying</creatorcontrib><creatorcontrib>Marcinkeviciene, Jovita</creatorcontrib><creatorcontrib>Kirby, Mark S.</creatorcontrib><creatorcontrib>Hamann, Lawrence G.</creatorcontrib><title>Seco-prolinenitrile inhibitors of dipeptidyl peptidase IV define minimal pharmacophore requirements at P1</title><title>Bioorganic & medicinal chemistry letters</title><addtitle>Bioorg Med Chem Lett</addtitle><description>The synthesis and dipeptidyl peptidase IV inhibitory activity of glycine- and alaninenitrile dipeptides are reported.
A series of seco-prolinenitrile-containing dipeptides were synthesized and assayed as inhibitors of the N-terminal sequence-specific serine protease dipeptidyl peptidase IV, a promising new target for treatment of type 2 diabetes. The inhibitors described herein assess the minimum structural requirements at P1 for this enzyme, resulting in the identification of inhibitors with low nM potency.</description><subject>Adenosine Deaminase - chemistry</subject><subject>Aniline Compounds - metabolism</subject><subject>Antidiabetic</subject><subject>Biological and medical sciences</subject><subject>Dipeptides - chemical synthesis</subject><subject>Dipeptides - chemistry</subject><subject>Dipeptides - pharmacology</subject><subject>Dipeptidyl Peptidase 4 - chemistry</subject><subject>Dipeptidyl peptidase IV</subject><subject>Enzyme inhibitors</subject><subject>Enzyme Inhibitors - chemical synthesis</subject><subject>Enzyme Inhibitors - chemistry</subject><subject>Enzyme Inhibitors - pharmacology</subject><subject>General and cellular metabolism. Vitamins</subject><subject>Glycoproteins - chemistry</subject><subject>Humans</subject><subject>Medical sciences</subject><subject>Nitriles - chemical synthesis</subject><subject>Nitriles - chemistry</subject><subject>Nitriles - pharmacology</subject><subject>Pharmacology. Drug treatments</subject><subject>Proline - chemistry</subject><subject>Serine protease</subject><issn>0960-894X</issn><issn>1464-3405</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2006</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqFkU9r3DAQxUVpSTZpvkAPRZfmZldjy5IMvYSQfxBIISH0JmR5xGqxLUfyBvLtq2UXcktOGml-b9C8R8gPYCUwEL83ZTfaoawYa0qAkrXqC1kBF7yoOWu-khVrBStUy_8dk5OUNowBZ5wfkWMQtRRMyhXxj2hDMccw-Aknv0Q_IPXT2nd-CTHR4GjvZ5wX378NdF-YhPTumfbosoaOfvKjyb21iaOxYV6HiDTiy9ZHHHFaEjUL_QvfyTdnhoRnh_OUPF1fPV3eFvcPN3eXF_eF5dAshWjbSkmQfeW4wo4zZ5TKFylF09lOclEZ6BFqhzWa2lnDBFSGI7iqy2-n5Hw_Nu_0ssW06NEni8NgJgzbpIUUtWiZ-hQEyRTUbZ3Bag_aGFKK6PQc88bxTQPTuyD0Ru-C0LsgNIDOQWTRz8P0bTdi_y45OJ-BXwfAJGsGF81kfXrnZNMIJXnm_uw5zJ69eow6WY-TxT7baxfdB__RP_4D9Jyo0w</recordid><startdate>20060315</startdate><enddate>20060315</enddate><creator>Magnin, David R.</creator><creator>Taunk, Prakash C.</creator><creator>Robertson, James G.</creator><creator>Wang, Aiying</creator><creator>Marcinkeviciene, Jovita</creator><creator>Kirby, Mark S.</creator><creator>Hamann, Lawrence G.</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>7QO</scope><scope>8FD</scope><scope>FR3</scope><scope>P64</scope><scope>7X8</scope></search><sort><creationdate>20060315</creationdate><title>Seco-prolinenitrile inhibitors of dipeptidyl peptidase IV define minimal pharmacophore requirements at P1</title><author>Magnin, David R. ; Taunk, Prakash C. ; Robertson, James G. ; Wang, Aiying ; Marcinkeviciene, Jovita ; Kirby, Mark S. ; Hamann, Lawrence G.</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c415t-69928717d2f48eb40fa88d2f7765bcb7462a1de13fe3ea3fca0612a4e1f2bfe3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2006</creationdate><topic>Adenosine Deaminase - chemistry</topic><topic>Aniline Compounds - metabolism</topic><topic>Antidiabetic</topic><topic>Biological and medical sciences</topic><topic>Dipeptides - chemical synthesis</topic><topic>Dipeptides - chemistry</topic><topic>Dipeptides - pharmacology</topic><topic>Dipeptidyl Peptidase 4 - chemistry</topic><topic>Dipeptidyl peptidase IV</topic><topic>Enzyme inhibitors</topic><topic>Enzyme Inhibitors - chemical synthesis</topic><topic>Enzyme Inhibitors - chemistry</topic><topic>Enzyme Inhibitors - pharmacology</topic><topic>General and cellular metabolism. Vitamins</topic><topic>Glycoproteins - chemistry</topic><topic>Humans</topic><topic>Medical sciences</topic><topic>Nitriles - chemical synthesis</topic><topic>Nitriles - chemistry</topic><topic>Nitriles - pharmacology</topic><topic>Pharmacology. Drug treatments</topic><topic>Proline - chemistry</topic><topic>Serine protease</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Magnin, David R.</creatorcontrib><creatorcontrib>Taunk, Prakash C.</creatorcontrib><creatorcontrib>Robertson, James G.</creatorcontrib><creatorcontrib>Wang, Aiying</creatorcontrib><creatorcontrib>Marcinkeviciene, Jovita</creatorcontrib><creatorcontrib>Kirby, Mark S.</creatorcontrib><creatorcontrib>Hamann, Lawrence G.</creatorcontrib><collection>Pascal-Francis</collection><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>Biotechnology Research Abstracts</collection><collection>Technology Research Database</collection><collection>Engineering Research Database</collection><collection>Biotechnology and BioEngineering Abstracts</collection><collection>MEDLINE - Academic</collection><jtitle>Bioorganic & medicinal chemistry letters</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Magnin, David R.</au><au>Taunk, Prakash C.</au><au>Robertson, James G.</au><au>Wang, Aiying</au><au>Marcinkeviciene, Jovita</au><au>Kirby, Mark S.</au><au>Hamann, Lawrence G.</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Seco-prolinenitrile inhibitors of dipeptidyl peptidase IV define minimal pharmacophore requirements at P1</atitle><jtitle>Bioorganic & medicinal chemistry letters</jtitle><addtitle>Bioorg Med Chem Lett</addtitle><date>2006-03-15</date><risdate>2006</risdate><volume>16</volume><issue>6</issue><spage>1731</spage><epage>1734</epage><pages>1731-1734</pages><issn>0960-894X</issn><eissn>1464-3405</eissn><abstract>The synthesis and dipeptidyl peptidase IV inhibitory activity of glycine- and alaninenitrile dipeptides are reported.
A series of seco-prolinenitrile-containing dipeptides were synthesized and assayed as inhibitors of the N-terminal sequence-specific serine protease dipeptidyl peptidase IV, a promising new target for treatment of type 2 diabetes. The inhibitors described herein assess the minimum structural requirements at P1 for this enzyme, resulting in the identification of inhibitors with low nM potency.</abstract><cop>Oxford</cop><pub>Elsevier Ltd</pub><pmid>16376077</pmid><doi>10.1016/j.bmcl.2005.11.098</doi><tpages>4</tpages></addata></record> |
| fulltext | fulltext |
| identifier | ISSN: 0960-894X |
| ispartof | Bioorganic & medicinal chemistry letters, 2006-03, Vol.16 (6), p.1731-1734 |
| issn | 0960-894X 1464-3405 |
| language | eng |
| recordid | cdi_proquest_miscellaneous_67636908 |
| source | MEDLINE; Elsevier ScienceDirect Journals Complete |
| subjects | Adenosine Deaminase - chemistry Aniline Compounds - metabolism Antidiabetic Biological and medical sciences Dipeptides - chemical synthesis Dipeptides - chemistry Dipeptides - pharmacology Dipeptidyl Peptidase 4 - chemistry Dipeptidyl peptidase IV Enzyme inhibitors Enzyme Inhibitors - chemical synthesis Enzyme Inhibitors - chemistry Enzyme Inhibitors - pharmacology General and cellular metabolism. Vitamins Glycoproteins - chemistry Humans Medical sciences Nitriles - chemical synthesis Nitriles - chemistry Nitriles - pharmacology Pharmacology. Drug treatments Proline - chemistry Serine protease |
| title | Seco-prolinenitrile inhibitors of dipeptidyl peptidase IV define minimal pharmacophore requirements at P1 |
| url | https://sfx.bib-bvb.de/sfx_tum?ctx_ver=Z39.88-2004&ctx_enc=info:ofi/enc:UTF-8&ctx_tim=2024-12-11T16%3A04%3A49IST&url_ver=Z39.88-2004&url_ctx_fmt=infofi/fmt:kev:mtx:ctx&rfr_id=info:sid/primo.exlibrisgroup.com:primo3-Article-proquest_cross&rft_val_fmt=info:ofi/fmt:kev:mtx:journal&rft.genre=article&rft.atitle=Seco-prolinenitrile%20inhibitors%20of%20dipeptidyl%20peptidase%20IV%20define%20minimal%20pharmacophore%20requirements%20at%20P1&rft.jtitle=Bioorganic%20&%20medicinal%20chemistry%20letters&rft.au=Magnin,%20David%20R.&rft.date=2006-03-15&rft.volume=16&rft.issue=6&rft.spage=1731&rft.epage=1734&rft.pages=1731-1734&rft.issn=0960-894X&rft.eissn=1464-3405&rft_id=info:doi/10.1016/j.bmcl.2005.11.098&rft_dat=%3Cproquest_cross%3E67636908%3C/proquest_cross%3E%3Curl%3E%3C/url%3E&disable_directlink=true&sfx.directlink=off&sfx.report_link=0&rft_id=info:oai/&rft_pqid=17081393&rft_id=info:pmid/16376077&rft_els_id=S0960894X05015349&rfr_iscdi=true |