Anthranilic Acid Based CCK1 Receptor Antagonists and CCK-8 Have a Common Step in Their “Receptor Desmodynamic Processes”
The interaction between the 1−47 N-terminus of the CCK1-R and the anthranilic acid based antagonists has been investigated by fluorescence spectroscopy. These antagonists interact with W39 of the N-terminal domain of the CCK1-R like that of the endogenous ligand CCK-8. This specific interaction was...
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| Veröffentlicht in: | Journal of medicinal chemistry 2006-04, Vol.49 (8), p.2456-2462 |
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| container_issue | 8 |
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| container_title | Journal of medicinal chemistry |
| container_volume | 49 |
| creator | De Luca, Stefania Saviano, Michele Lassiani, Lucia Yannakopoulou, Konstantina Stefanidou, Penny Aloj, Luigi Morelli, Giancarlo Varnavas, Antonio |
| description | The interaction between the 1−47 N-terminus of the CCK1-R and the anthranilic acid based antagonists has been investigated by fluorescence spectroscopy. These antagonists interact with W39 of the N-terminal domain of the CCK1-R like that of the endogenous ligand CCK-8. This specific interaction was not found in other nonpeptide ligands of the CCK1-R. Conformational studies, using NMR and energy minimization procedures, have allowed formulation of a new hypothesis on the CCK1-R binding mode of the anthranilic antagonists. |
| doi_str_mv | 10.1021/jm051050n |
| format | Article |
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These antagonists interact with W39 of the N-terminal domain of the CCK1-R like that of the endogenous ligand CCK-8. This specific interaction was not found in other nonpeptide ligands of the CCK1-R. Conformational studies, using NMR and energy minimization procedures, have allowed formulation of a new hypothesis on the CCK1-R binding mode of the anthranilic antagonists.</description><identifier>ISSN: 0022-2623</identifier><identifier>EISSN: 1520-4804</identifier><identifier>DOI: 10.1021/jm051050n</identifier><identifier>PMID: 16610788</identifier><identifier>CODEN: JMCMAR</identifier><language>eng</language><publisher>Washington, DC: American Chemical Society</publisher><subject>Animals ; Binding, Competitive - drug effects ; Biological and medical sciences ; Biological Assay ; Humans ; Indoles - chemistry ; Indoles - pharmacology ; Ligands ; Magnetic Resonance Spectroscopy ; Medical sciences ; Models, Molecular ; Molecular Structure ; Neuropharmacology ; Neurotransmitters. 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Drug treatments ; Proglumide - analogs & derivatives ; Proglumide - chemistry ; Proglumide - pharmacology ; Protein Conformation ; Rats ; Receptor, Cholecystokinin A - antagonists & inhibitors ; Receptor, Cholecystokinin A - chemistry ; Sincalide - chemistry ; Sincalide - pharmacology ; Spectrometry, Fluorescence ; Structure-Activity Relationship</subject><ispartof>Journal of medicinal chemistry, 2006-04, Vol.49 (8), p.2456-2462</ispartof><rights>Copyright © 2006 American Chemical Society</rights><rights>2006 INIST-CNRS</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://pubs.acs.org/doi/pdf/10.1021/jm051050n$$EPDF$$P50$$Gacs$$H</linktopdf><linktohtml>$$Uhttps://pubs.acs.org/doi/10.1021/jm051050n$$EHTML$$P50$$Gacs$$H</linktohtml><link.rule.ids>314,777,781,27057,27905,27906,56719,56769</link.rule.ids><backlink>$$Uhttp://pascal-francis.inist.fr/vibad/index.php?action=getRecordDetail&idt=17707995$$DView record in Pascal Francis$$Hfree_for_read</backlink><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/16610788$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>De Luca, Stefania</creatorcontrib><creatorcontrib>Saviano, Michele</creatorcontrib><creatorcontrib>Lassiani, Lucia</creatorcontrib><creatorcontrib>Yannakopoulou, Konstantina</creatorcontrib><creatorcontrib>Stefanidou, Penny</creatorcontrib><creatorcontrib>Aloj, Luigi</creatorcontrib><creatorcontrib>Morelli, Giancarlo</creatorcontrib><creatorcontrib>Varnavas, Antonio</creatorcontrib><title>Anthranilic Acid Based CCK1 Receptor Antagonists and CCK-8 Have a Common Step in Their “Receptor Desmodynamic Processes”</title><title>Journal of medicinal chemistry</title><addtitle>J. Med. Chem</addtitle><description>The interaction between the 1−47 N-terminus of the CCK1-R and the anthranilic acid based antagonists has been investigated by fluorescence spectroscopy. These antagonists interact with W39 of the N-terminal domain of the CCK1-R like that of the endogenous ligand CCK-8. This specific interaction was not found in other nonpeptide ligands of the CCK1-R. Conformational studies, using NMR and energy minimization procedures, have allowed formulation of a new hypothesis on the CCK1-R binding mode of the anthranilic antagonists.</description><subject>Animals</subject><subject>Binding, Competitive - drug effects</subject><subject>Biological and medical sciences</subject><subject>Biological Assay</subject><subject>Humans</subject><subject>Indoles - chemistry</subject><subject>Indoles - pharmacology</subject><subject>Ligands</subject><subject>Magnetic Resonance Spectroscopy</subject><subject>Medical sciences</subject><subject>Models, Molecular</subject><subject>Molecular Structure</subject><subject>Neuropharmacology</subject><subject>Neurotransmitters. Neurotransmission. Receptors</subject><subject>ortho-Aminobenzoates - chemistry</subject><subject>ortho-Aminobenzoates - pharmacology</subject><subject>Pancreas - drug effects</subject><subject>Pancreas - metabolism</subject><subject>Peptidergic system (neuropeptide, opioid peptide, opiates...). Adenosinergic and purinergic systems</subject><subject>Pharmacology. Drug treatments</subject><subject>Proglumide - analogs & derivatives</subject><subject>Proglumide - chemistry</subject><subject>Proglumide - pharmacology</subject><subject>Protein Conformation</subject><subject>Rats</subject><subject>Receptor, Cholecystokinin A - antagonists & inhibitors</subject><subject>Receptor, Cholecystokinin A - chemistry</subject><subject>Sincalide - chemistry</subject><subject>Sincalide - pharmacology</subject><subject>Spectrometry, Fluorescence</subject><subject>Structure-Activity Relationship</subject><issn>0022-2623</issn><issn>1520-4804</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2006</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNpFkc1u1DAUhS1ERYfCghdA3tBd4NqO_5ZDKBTRQtUOGzaWG9_QDIkzxBlEJRZ9EHi5Pknddpiu7uJ89xzdcwl5weA1A87eLHuQDCTER2TGJIeiNFA-JjMAzguuuNglT1NaAoBgXDwhu0wpBtqYGfkzj9PF6GPbtTWd122gb33CQKvqE6OnWONqGkaaIf99iG2aEvXxTi0MPfS_kHpaDX0_RHo24Yq2kS4usB3p9dXf7fY7TP0QLqPvc8bJONSYEqbrq3_PyE7ju4TPN3OPfH1_sKgOi6MvHz5W86PCC9BTUTJug9HWBBmY4SE04ZxbJdCWWJdByrJRWitoLDQ8NJ6XBkFgaVTgHLgVe2T_3nc1Dj_XmCbXt6nGrvMRh3VyShtphWUZfLkB1-c9Brca296Pl-5_Xxl4tQF8qn3X5ObqNj1wWoO2VmauuOdyZfh7q_vxRw4TWrrFyZk7Pf6cT_t27NSDr6-TWw7rMeY-HAN3-1-3_a-4ASKRlBI</recordid><startdate>20060420</startdate><enddate>20060420</enddate><creator>De Luca, Stefania</creator><creator>Saviano, Michele</creator><creator>Lassiani, Lucia</creator><creator>Yannakopoulou, Konstantina</creator><creator>Stefanidou, Penny</creator><creator>Aloj, Luigi</creator><creator>Morelli, Giancarlo</creator><creator>Varnavas, Antonio</creator><general>American Chemical Society</general><scope>BSCLL</scope><scope>IQODW</scope><scope>CGR</scope><scope>CUY</scope><scope>CVF</scope><scope>ECM</scope><scope>EIF</scope><scope>NPM</scope><scope>7X8</scope></search><sort><creationdate>20060420</creationdate><title>Anthranilic Acid Based CCK1 Receptor Antagonists and CCK-8 Have a Common Step in Their “Receptor Desmodynamic Processes”</title><author>De Luca, Stefania ; Saviano, Michele ; Lassiani, Lucia ; Yannakopoulou, Konstantina ; Stefanidou, Penny ; Aloj, Luigi ; Morelli, Giancarlo ; Varnavas, Antonio</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-a307t-4129d8798d5d182ddfdb2963e94ec4d554f67760f90f2dfa248e03e486d220293</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2006</creationdate><topic>Animals</topic><topic>Binding, Competitive - drug effects</topic><topic>Biological and medical sciences</topic><topic>Biological Assay</topic><topic>Humans</topic><topic>Indoles - chemistry</topic><topic>Indoles - pharmacology</topic><topic>Ligands</topic><topic>Magnetic Resonance Spectroscopy</topic><topic>Medical sciences</topic><topic>Models, Molecular</topic><topic>Molecular Structure</topic><topic>Neuropharmacology</topic><topic>Neurotransmitters. Neurotransmission. Receptors</topic><topic>ortho-Aminobenzoates - chemistry</topic><topic>ortho-Aminobenzoates - pharmacology</topic><topic>Pancreas - drug effects</topic><topic>Pancreas - metabolism</topic><topic>Peptidergic system (neuropeptide, opioid peptide, opiates...). Adenosinergic and purinergic systems</topic><topic>Pharmacology. Drug treatments</topic><topic>Proglumide - analogs & derivatives</topic><topic>Proglumide - chemistry</topic><topic>Proglumide - pharmacology</topic><topic>Protein Conformation</topic><topic>Rats</topic><topic>Receptor, Cholecystokinin A - antagonists & inhibitors</topic><topic>Receptor, Cholecystokinin A - chemistry</topic><topic>Sincalide - chemistry</topic><topic>Sincalide - pharmacology</topic><topic>Spectrometry, Fluorescence</topic><topic>Structure-Activity Relationship</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>De Luca, Stefania</creatorcontrib><creatorcontrib>Saviano, Michele</creatorcontrib><creatorcontrib>Lassiani, Lucia</creatorcontrib><creatorcontrib>Yannakopoulou, Konstantina</creatorcontrib><creatorcontrib>Stefanidou, Penny</creatorcontrib><creatorcontrib>Aloj, Luigi</creatorcontrib><creatorcontrib>Morelli, Giancarlo</creatorcontrib><creatorcontrib>Varnavas, Antonio</creatorcontrib><collection>Istex</collection><collection>Pascal-Francis</collection><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>MEDLINE - Academic</collection><jtitle>Journal of medicinal chemistry</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>De Luca, Stefania</au><au>Saviano, Michele</au><au>Lassiani, Lucia</au><au>Yannakopoulou, Konstantina</au><au>Stefanidou, Penny</au><au>Aloj, Luigi</au><au>Morelli, Giancarlo</au><au>Varnavas, Antonio</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Anthranilic Acid Based CCK1 Receptor Antagonists and CCK-8 Have a Common Step in Their “Receptor Desmodynamic Processes”</atitle><jtitle>Journal of medicinal chemistry</jtitle><addtitle>J. Med. Chem</addtitle><date>2006-04-20</date><risdate>2006</risdate><volume>49</volume><issue>8</issue><spage>2456</spage><epage>2462</epage><pages>2456-2462</pages><issn>0022-2623</issn><eissn>1520-4804</eissn><coden>JMCMAR</coden><abstract>The interaction between the 1−47 N-terminus of the CCK1-R and the anthranilic acid based antagonists has been investigated by fluorescence spectroscopy. These antagonists interact with W39 of the N-terminal domain of the CCK1-R like that of the endogenous ligand CCK-8. This specific interaction was not found in other nonpeptide ligands of the CCK1-R. Conformational studies, using NMR and energy minimization procedures, have allowed formulation of a new hypothesis on the CCK1-R binding mode of the anthranilic antagonists.</abstract><cop>Washington, DC</cop><pub>American Chemical Society</pub><pmid>16610788</pmid><doi>10.1021/jm051050n</doi><tpages>7</tpages></addata></record> |
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| subjects | Animals Binding, Competitive - drug effects Biological and medical sciences Biological Assay Humans Indoles - chemistry Indoles - pharmacology Ligands Magnetic Resonance Spectroscopy Medical sciences Models, Molecular Molecular Structure Neuropharmacology Neurotransmitters. Neurotransmission. Receptors ortho-Aminobenzoates - chemistry ortho-Aminobenzoates - pharmacology Pancreas - drug effects Pancreas - metabolism Peptidergic system (neuropeptide, opioid peptide, opiates...). Adenosinergic and purinergic systems Pharmacology. Drug treatments Proglumide - analogs & derivatives Proglumide - chemistry Proglumide - pharmacology Protein Conformation Rats Receptor, Cholecystokinin A - antagonists & inhibitors Receptor, Cholecystokinin A - chemistry Sincalide - chemistry Sincalide - pharmacology Spectrometry, Fluorescence Structure-Activity Relationship |
| title | Anthranilic Acid Based CCK1 Receptor Antagonists and CCK-8 Have a Common Step in Their “Receptor Desmodynamic Processes” |
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