In-silico characterization of ECE-1 inhibitors
Abstract Atherosclerosis is the primary cause of CAD and cerebrovascular disease. Endothelin (ET)-1 is a vasoconstrictive peptide implicated in Atherosclerosis pathology. Endothelin-converting enzyme (ECE) is a membrane metalloprotease that generates endothelin. Reported inhibitors of ECE-1 and thei...
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| Veröffentlicht in: | Computers in biology and medicine 2012-04, Vol.42 (4), p.446-457 |
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| creator | Ajay Babu, P Colluru, Viswa Teja S.S Anaparthy, Naishitha |
| description | Abstract Atherosclerosis is the primary cause of CAD and cerebrovascular disease. Endothelin (ET)-1 is a vasoconstrictive peptide implicated in Atherosclerosis pathology. Endothelin-converting enzyme (ECE) is a membrane metalloprotease that generates endothelin. Reported inhibitors of ECE-1 and their IC50 values were retrieved from literature and their structures were docked with the parent protein using the Molegro virtual docker. The obtained MolDock scores of each of the compounds are hereby reported and are subject to graphical analysis in conjunction with their respective IC50 values to characterize potent inhibitors. A search was then run in the ZINC database for compounds with similar properties. Potent inhibitors with higher Dock scores and better Ranking were isolated and are reported. |
| doi_str_mv | 10.1016/j.compbiomed.2011.12.013 |
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Endothelin (ET)-1 is a vasoconstrictive peptide implicated in Atherosclerosis pathology. Endothelin-converting enzyme (ECE) is a membrane metalloprotease that generates endothelin. Reported inhibitors of ECE-1 and their IC50 values were retrieved from literature and their structures were docked with the parent protein using the Molegro virtual docker. The obtained MolDock scores of each of the compounds are hereby reported and are subject to graphical analysis in conjunction with their respective IC50 values to characterize potent inhibitors. A search was then run in the ZINC database for compounds with similar properties. Potent inhibitors with higher Dock scores and better Ranking were isolated and are reported.</description><identifier>ISSN: 0010-4825</identifier><identifier>EISSN: 1879-0534</identifier><identifier>DOI: 10.1016/j.compbiomed.2011.12.013</identifier><identifier>PMID: 22245098</identifier><identifier>CODEN: CBMDAW</identifier><language>eng</language><publisher>United States: Elsevier Ltd</publisher><subject>Algorithms ; Aspartic Acid Endopeptidases - antagonists & inhibitors ; Aspartic Acid Endopeptidases - chemistry ; Aspartic Acid Endopeptidases - metabolism ; Atherosclerosis ; Binding sites ; Blood pressure ; Cardiovascular disease ; Cholesterol ; Colleges & universities ; Crystal structure ; Databases, Protein ; Docking ; ECE-1 ; Endothelin ; Endothelin converting enzyme ; Endothelin-1 - metabolism ; Endothelin-Converting Enzymes ; Endothelium ; Enzyme Inhibitors - chemistry ; Enzyme Inhibitors - pharmacology ; Glycopeptides - chemistry ; Glycopeptides - metabolism ; Graduate students ; Humans ; Hydrogen Bonding ; Hydrogen bonds ; Hypertension ; In-silico characterization ; Inhibition ; Inhibitory Concentration 50 ; Internal Medicine ; Life sciences ; Ligands ; Metalloendopeptidases - antagonists & inhibitors ; Metalloendopeptidases - chemistry ; Metalloendopeptidases - metabolism ; Molecular Dynamics Simulation ; Molecular weight ; Molegro virtual docker ; Other ; Protein Binding ; Software ; Structure-Activity Relationship ; TSAR</subject><ispartof>Computers in biology and medicine, 2012-04, Vol.42 (4), p.446-457</ispartof><rights>Elsevier Ltd</rights><rights>2012 Elsevier Ltd</rights><rights>Copyright © 2012 Elsevier Ltd. All rights reserved.</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c456t-6120796da03f28f55d05152cb310ce11993da0985d7dfac398ebca770b14d15a3</citedby><cites>FETCH-LOGICAL-c456t-6120796da03f28f55d05152cb310ce11993da0985d7dfac398ebca770b14d15a3</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktohtml>$$Uhttps://www.sciencedirect.com/science/article/pii/S0010482511002538$$EHTML$$P50$$Gelsevier$$H</linktohtml><link.rule.ids>314,776,780,3537,27901,27902,65306</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/22245098$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Ajay Babu, P</creatorcontrib><creatorcontrib>Colluru, Viswa Teja S.S</creatorcontrib><creatorcontrib>Anaparthy, Naishitha</creatorcontrib><title>In-silico characterization of ECE-1 inhibitors</title><title>Computers in biology and medicine</title><addtitle>Comput Biol Med</addtitle><description>Abstract Atherosclerosis is the primary cause of CAD and cerebrovascular disease. Endothelin (ET)-1 is a vasoconstrictive peptide implicated in Atherosclerosis pathology. Endothelin-converting enzyme (ECE) is a membrane metalloprotease that generates endothelin. Reported inhibitors of ECE-1 and their IC50 values were retrieved from literature and their structures were docked with the parent protein using the Molegro virtual docker. The obtained MolDock scores of each of the compounds are hereby reported and are subject to graphical analysis in conjunction with their respective IC50 values to characterize potent inhibitors. A search was then run in the ZINC database for compounds with similar properties. Potent inhibitors with higher Dock scores and better Ranking were isolated and are reported.</description><subject>Algorithms</subject><subject>Aspartic Acid Endopeptidases - antagonists & inhibitors</subject><subject>Aspartic Acid Endopeptidases - chemistry</subject><subject>Aspartic Acid Endopeptidases - metabolism</subject><subject>Atherosclerosis</subject><subject>Binding sites</subject><subject>Blood pressure</subject><subject>Cardiovascular disease</subject><subject>Cholesterol</subject><subject>Colleges & universities</subject><subject>Crystal structure</subject><subject>Databases, Protein</subject><subject>Docking</subject><subject>ECE-1</subject><subject>Endothelin</subject><subject>Endothelin converting enzyme</subject><subject>Endothelin-1 - metabolism</subject><subject>Endothelin-Converting Enzymes</subject><subject>Endothelium</subject><subject>Enzyme Inhibitors - chemistry</subject><subject>Enzyme Inhibitors - pharmacology</subject><subject>Glycopeptides - chemistry</subject><subject>Glycopeptides - metabolism</subject><subject>Graduate students</subject><subject>Humans</subject><subject>Hydrogen Bonding</subject><subject>Hydrogen bonds</subject><subject>Hypertension</subject><subject>In-silico characterization</subject><subject>Inhibition</subject><subject>Inhibitory Concentration 50</subject><subject>Internal Medicine</subject><subject>Life sciences</subject><subject>Ligands</subject><subject>Metalloendopeptidases - antagonists & inhibitors</subject><subject>Metalloendopeptidases - chemistry</subject><subject>Metalloendopeptidases - metabolism</subject><subject>Molecular Dynamics Simulation</subject><subject>Molecular weight</subject><subject>Molegro virtual docker</subject><subject>Other</subject><subject>Protein Binding</subject><subject>Software</subject><subject>Structure-Activity Relationship</subject><subject>TSAR</subject><issn>0010-4825</issn><issn>1879-0534</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2012</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><sourceid>8G5</sourceid><sourceid>BENPR</sourceid><sourceid>GUQSH</sourceid><sourceid>M2O</sourceid><recordid>eNqNkU1LxDAQhoMoun78BSl48NQ6kzTb5CLosn6A4EE9hzRNMWu3WZOusP56U1YRPHnKYZ53JvMMIRlCgYDTi0Vh_HJVO7-0TUEBsUBaALIdMkFRyRw4K3fJBAAhLwXlB-QwxgUAlMBgnxxQSksOUkxIcd_n0XXO-My86qDNYIP71IPzfebbbD6b55i5_tXVbvAhHpO9VnfRnny_R-TlZv48u8sfHm_vZ1cPuSn5dMinSKGS00YDa6loOW-AI6emZgjGIkrJUk0K3lRNqw2TwtZGVxXUWDbINTsi59u-q-Df1zYOaumisV2ne-vXUUkqWAWVEIk8-0Mu_Dr06XMKgTEUHFAmSmwpE3yMwbZqFdxSh02C1KhULdSvUjUqVUhVUpqip98D1vVY-wn-OEzA9RawSciHs0FF42xvbOOCNYNqvPvPlMs_TUznemd092Y3Nv7upGIKqKfxtONlEQEoZ4J9AX2dnnw</recordid><startdate>20120401</startdate><enddate>20120401</enddate><creator>Ajay Babu, P</creator><creator>Colluru, Viswa Teja S.S</creator><creator>Anaparthy, Naishitha</creator><general>Elsevier Ltd</general><general>Elsevier Limited</general><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>3V.</scope><scope>7RV</scope><scope>7X7</scope><scope>7XB</scope><scope>88E</scope><scope>8AL</scope><scope>8AO</scope><scope>8FD</scope><scope>8FE</scope><scope>8FG</scope><scope>8FH</scope><scope>8FI</scope><scope>8FJ</scope><scope>8FK</scope><scope>8G5</scope><scope>ABUWG</scope><scope>AFKRA</scope><scope>ARAPS</scope><scope>AZQEC</scope><scope>BBNVY</scope><scope>BENPR</scope><scope>BGLVJ</scope><scope>BHPHI</scope><scope>CCPQU</scope><scope>DWQXO</scope><scope>FR3</scope><scope>FYUFA</scope><scope>GHDGH</scope><scope>GNUQQ</scope><scope>GUQSH</scope><scope>HCIFZ</scope><scope>JQ2</scope><scope>K7-</scope><scope>K9.</scope><scope>KB0</scope><scope>LK8</scope><scope>M0N</scope><scope>M0S</scope><scope>M1P</scope><scope>M2O</scope><scope>M7P</scope><scope>M7Z</scope><scope>MBDVC</scope><scope>NAPCQ</scope><scope>P5Z</scope><scope>P62</scope><scope>P64</scope><scope>PQEST</scope><scope>PQQKQ</scope><scope>PQUKI</scope><scope>PRINS</scope><scope>Q9U</scope><scope>7X8</scope></search><sort><creationdate>20120401</creationdate><title>In-silico characterization of ECE-1 inhibitors</title><author>Ajay Babu, P ; Colluru, Viswa Teja S.S ; Anaparthy, Naishitha</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c456t-6120796da03f28f55d05152cb310ce11993da0985d7dfac398ebca770b14d15a3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2012</creationdate><topic>Algorithms</topic><topic>Aspartic Acid Endopeptidases - antagonists & inhibitors</topic><topic>Aspartic Acid Endopeptidases - chemistry</topic><topic>Aspartic Acid Endopeptidases - metabolism</topic><topic>Atherosclerosis</topic><topic>Binding sites</topic><topic>Blood pressure</topic><topic>Cardiovascular disease</topic><topic>Cholesterol</topic><topic>Colleges & universities</topic><topic>Crystal structure</topic><topic>Databases, Protein</topic><topic>Docking</topic><topic>ECE-1</topic><topic>Endothelin</topic><topic>Endothelin converting enzyme</topic><topic>Endothelin-1 - metabolism</topic><topic>Endothelin-Converting Enzymes</topic><topic>Endothelium</topic><topic>Enzyme Inhibitors - chemistry</topic><topic>Enzyme Inhibitors - pharmacology</topic><topic>Glycopeptides - chemistry</topic><topic>Glycopeptides - metabolism</topic><topic>Graduate students</topic><topic>Humans</topic><topic>Hydrogen Bonding</topic><topic>Hydrogen bonds</topic><topic>Hypertension</topic><topic>In-silico characterization</topic><topic>Inhibition</topic><topic>Inhibitory Concentration 50</topic><topic>Internal Medicine</topic><topic>Life sciences</topic><topic>Ligands</topic><topic>Metalloendopeptidases - 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Endothelin (ET)-1 is a vasoconstrictive peptide implicated in Atherosclerosis pathology. Endothelin-converting enzyme (ECE) is a membrane metalloprotease that generates endothelin. Reported inhibitors of ECE-1 and their IC50 values were retrieved from literature and their structures were docked with the parent protein using the Molegro virtual docker. The obtained MolDock scores of each of the compounds are hereby reported and are subject to graphical analysis in conjunction with their respective IC50 values to characterize potent inhibitors. A search was then run in the ZINC database for compounds with similar properties. Potent inhibitors with higher Dock scores and better Ranking were isolated and are reported.</abstract><cop>United States</cop><pub>Elsevier Ltd</pub><pmid>22245098</pmid><doi>10.1016/j.compbiomed.2011.12.013</doi><tpages>12</tpages></addata></record> |
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| subjects | Algorithms Aspartic Acid Endopeptidases - antagonists & inhibitors Aspartic Acid Endopeptidases - chemistry Aspartic Acid Endopeptidases - metabolism Atherosclerosis Binding sites Blood pressure Cardiovascular disease Cholesterol Colleges & universities Crystal structure Databases, Protein Docking ECE-1 Endothelin Endothelin converting enzyme Endothelin-1 - metabolism Endothelin-Converting Enzymes Endothelium Enzyme Inhibitors - chemistry Enzyme Inhibitors - pharmacology Glycopeptides - chemistry Glycopeptides - metabolism Graduate students Humans Hydrogen Bonding Hydrogen bonds Hypertension In-silico characterization Inhibition Inhibitory Concentration 50 Internal Medicine Life sciences Ligands Metalloendopeptidases - antagonists & inhibitors Metalloendopeptidases - chemistry Metalloendopeptidases - metabolism Molecular Dynamics Simulation Molecular weight Molegro virtual docker Other Protein Binding Software Structure-Activity Relationship TSAR |
| title | In-silico characterization of ECE-1 inhibitors |
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