Selection of single-stranded DNA molecules that bind and inhibit human thrombin
APTAMERS 1 are double-stranded DNA or single-stranded RNA molecules that bind specific molecular targets. Large randomly generated populations can be enriched in aptamers by in vitro selection and polymerase chain reaction 1–11 . But so far single-stranded DNA has not been investigated for aptamer p...
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| Veröffentlicht in: | Nature (London) 1992-02, Vol.355 (6360), p.564-566 |
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| creator | Bock, Louis C Griffin, Linda C Latham, John A Vermaas, Eric H Toole, John J |
| description | APTAMERS
1
are double-stranded DNA or single-stranded RNA molecules that bind specific molecular targets. Large randomly generated populations can be enriched in aptamers by
in vitro
selection and polymerase chain reaction
1–11
. But so far single-stranded DNA has not been investigated for aptamer properties, nor has a target protein been considered that does not interact physiologically with nucleic acid. Here we describe the isolation of single-stranded DNA aptamers to the protease thrombin of the blood coagulation cascade and report binding affinities in the range 25–200 nM. Sequence data from 32 thrsombin aptamers, selected from a pool of DNA containing 60 nucleotides of random sequence, displayed a highly conserved 14–17–base region. Several of these aptamers at nanomolar concentrations inhibited thrombin-catalysed fibrin-clot formation
in vitro
using either purified fibrinogen or human plasma. |
| doi_str_mv | 10.1038/355564a0 |
| format | Article |
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1
are double-stranded DNA or single-stranded RNA molecules that bind specific molecular targets. Large randomly generated populations can be enriched in aptamers by
in vitro
selection and polymerase chain reaction
1–11
. But so far single-stranded DNA has not been investigated for aptamer properties, nor has a target protein been considered that does not interact physiologically with nucleic acid. Here we describe the isolation of single-stranded DNA aptamers to the protease thrombin of the blood coagulation cascade and report binding affinities in the range 25–200 nM. Sequence data from 32 thrsombin aptamers, selected from a pool of DNA containing 60 nucleotides of random sequence, displayed a highly conserved 14–17–base region. Several of these aptamers at nanomolar concentrations inhibited thrombin-catalysed fibrin-clot formation
in vitro
using either purified fibrinogen or human plasma.</description><identifier>ISSN: 0028-0836</identifier><identifier>EISSN: 1476-4687</identifier><identifier>DOI: 10.1038/355564a0</identifier><identifier>PMID: 1741036</identifier><identifier>CODEN: NATUAS</identifier><language>eng</language><publisher>London: Nature Publishing Group UK</publisher><subject>Analytical, structural and metabolic biochemistry ; Base Sequence ; Biological and medical sciences ; Blood ; Blood Coagulation - drug effects ; Cloning, Molecular ; Coagulation ; Deoxyribonucleic acid ; DNA ; DNA, Single-Stranded - isolation & purification ; Dose-Response Relationship, Drug ; Enzymes and enzyme inhibitors ; Fundamental and applied biological sciences. Psychology ; Humanities and Social Sciences ; Humans ; Hydrolases ; In Vitro Techniques ; letter ; Medical research ; Molecular Sequence Data ; multidisciplinary ; Nucleic acids ; Polymerase Chain Reaction ; Science ; Science (multidisciplinary) ; Sequence Homology, Nucleic Acid ; Thrombin - antagonists & inhibitors ; Thrombin Time</subject><ispartof>Nature (London), 1992-02, Vol.355 (6360), p.564-566</ispartof><rights>Springer Nature Limited 1992</rights><rights>1992 INIST-CNRS</rights><rights>Copyright Macmillan Journals Ltd. Feb 6, 1992</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c454t-c96f0fbcda3236daff47dca0e2e5d20e20e2f1df0e30fe6344ce38afa621e56a3</citedby><cites>FETCH-LOGICAL-c454t-c96f0fbcda3236daff47dca0e2e5d20e20e2f1df0e30fe6344ce38afa621e56a3</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://link.springer.com/content/pdf/10.1038/355564a0$$EPDF$$P50$$Gspringer$$H</linktopdf><linktohtml>$$Uhttps://link.springer.com/10.1038/355564a0$$EHTML$$P50$$Gspringer$$H</linktohtml><link.rule.ids>314,780,784,2727,27924,27925,41488,42557,51319</link.rule.ids><backlink>$$Uhttp://pascal-francis.inist.fr/vibad/index.php?action=getRecordDetail&idt=5194273$$DView record in Pascal Francis$$Hfree_for_read</backlink><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/1741036$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Bock, Louis C</creatorcontrib><creatorcontrib>Griffin, Linda C</creatorcontrib><creatorcontrib>Latham, John A</creatorcontrib><creatorcontrib>Vermaas, Eric H</creatorcontrib><creatorcontrib>Toole, John J</creatorcontrib><title>Selection of single-stranded DNA molecules that bind and inhibit human thrombin</title><title>Nature (London)</title><addtitle>Nature</addtitle><addtitle>Nature</addtitle><description>APTAMERS
1
are double-stranded DNA or single-stranded RNA molecules that bind specific molecular targets. Large randomly generated populations can be enriched in aptamers by
in vitro
selection and polymerase chain reaction
1–11
. But so far single-stranded DNA has not been investigated for aptamer properties, nor has a target protein been considered that does not interact physiologically with nucleic acid. Here we describe the isolation of single-stranded DNA aptamers to the protease thrombin of the blood coagulation cascade and report binding affinities in the range 25–200 nM. Sequence data from 32 thrsombin aptamers, selected from a pool of DNA containing 60 nucleotides of random sequence, displayed a highly conserved 14–17–base region. Several of these aptamers at nanomolar concentrations inhibited thrombin-catalysed fibrin-clot formation
in vitro
using either purified fibrinogen or human plasma.</description><subject>Analytical, structural and metabolic biochemistry</subject><subject>Base Sequence</subject><subject>Biological and medical sciences</subject><subject>Blood</subject><subject>Blood Coagulation - drug effects</subject><subject>Cloning, Molecular</subject><subject>Coagulation</subject><subject>Deoxyribonucleic acid</subject><subject>DNA</subject><subject>DNA, Single-Stranded - isolation & purification</subject><subject>Dose-Response Relationship, Drug</subject><subject>Enzymes and enzyme inhibitors</subject><subject>Fundamental and applied biological sciences. Psychology</subject><subject>Humanities and Social Sciences</subject><subject>Humans</subject><subject>Hydrolases</subject><subject>In Vitro Techniques</subject><subject>letter</subject><subject>Medical research</subject><subject>Molecular Sequence Data</subject><subject>multidisciplinary</subject><subject>Nucleic acids</subject><subject>Polymerase Chain Reaction</subject><subject>Science</subject><subject>Science (multidisciplinary)</subject><subject>Sequence Homology, Nucleic Acid</subject><subject>Thrombin - antagonists & inhibitors</subject><subject>Thrombin Time</subject><issn>0028-0836</issn><issn>1476-4687</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1992</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><sourceid>8G5</sourceid><sourceid>ABUWG</sourceid><sourceid>AFKRA</sourceid><sourceid>AZQEC</sourceid><sourceid>BEC</sourceid><sourceid>BENPR</sourceid><sourceid>CCPQU</sourceid><sourceid>DWQXO</sourceid><sourceid>GNUQQ</sourceid><sourceid>GUQSH</sourceid><sourceid>M2O</sourceid><recordid>eNqF0U1rFTEUBuAglnpbBf-AEqT4sRjNd-YuS6tVKHahrofc5KQ3ZSZTk5mF_76nzPUWRBRCsnifnJNwCHnO2XvOZPtBaq2NcuwRWXFlTaNMax-TFWOibVgrzRNyVOsNY0xzqw7JIe54z6zI1TfowU9pzHSMtKZ83UNTp-JygEDPv57SYUQw91DptHUT3aQcKKY05W3apIlu58FlzMo4YPaUHETXV3i2O4_Jj08fv599bi6vLr6cnV42Xmk1NX5tIosbH5wU0gQXo7LBOwYCdBB44Io8RAaSRTBSKQ-yddEZwUEbJ4_Jm6XubRl_zlCnbkjVQ9-7DONcO6vwjlVKoHz9bylaZtba_hdyw1EKjvDVH_BmnEvG73aCYctW23v0dkG-jLUWiN1tSYMrvzrOuvuZdb9nhvTFrt68GSA8wGVImJ_scle96yMOx6e6Z5qvlbAS2buFVUzyNZSHZ_2l5cvFZjfNBfa19uAOQCWz_Q</recordid><startdate>19920206</startdate><enddate>19920206</enddate><creator>Bock, Louis C</creator><creator>Griffin, Linda C</creator><creator>Latham, John A</creator><creator>Vermaas, Eric H</creator><creator>Toole, John J</creator><general>Nature Publishing Group UK</general><general>Nature Publishing</general><general>Nature Publishing Group</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>3V.</scope><scope>7QG</scope><scope>7QL</scope><scope>7QP</scope><scope>7QR</scope><scope>7RV</scope><scope>7SN</scope><scope>7SS</scope><scope>7ST</scope><scope>7T5</scope><scope>7TG</scope><scope>7TK</scope><scope>7TM</scope><scope>7TO</scope><scope>7U9</scope><scope>7X2</scope><scope>7X7</scope><scope>7XB</scope><scope>88A</scope><scope>88E</scope><scope>88G</scope><scope>88I</scope><scope>8AF</scope><scope>8AO</scope><scope>8C1</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>ABJCF</scope><scope>ABUWG</scope><scope>AFKRA</scope><scope>ARAPS</scope><scope>ATCPS</scope><scope>AZQEC</scope><scope>BBNVY</scope><scope>BEC</scope><scope>BENPR</scope><scope>BGLVJ</scope><scope>BHPHI</scope><scope>BKSAR</scope><scope>C1K</scope><scope>CCPQU</scope><scope>D1I</scope><scope>DWQXO</scope><scope>FR3</scope><scope>FYUFA</scope><scope>GHDGH</scope><scope>GNUQQ</scope><scope>GUQSH</scope><scope>H94</scope><scope>HCIFZ</scope><scope>K9.</scope><scope>KB.</scope><scope>KB0</scope><scope>KL.</scope><scope>L6V</scope><scope>LK8</scope><scope>M0K</scope><scope>M0S</scope><scope>M1P</scope><scope>M2M</scope><scope>M2O</scope><scope>M2P</scope><scope>M7N</scope><scope>M7P</scope><scope>M7S</scope><scope>MBDVC</scope><scope>NAPCQ</scope><scope>P5Z</scope><scope>P62</scope><scope>P64</scope><scope>PATMY</scope><scope>PCBAR</scope><scope>PDBOC</scope><scope>PQEST</scope><scope>PQQKQ</scope><scope>PQUKI</scope><scope>PSYQQ</scope><scope>PTHSS</scope><scope>PYCSY</scope><scope>Q9U</scope><scope>R05</scope><scope>RC3</scope><scope>S0X</scope><scope>SOI</scope><scope>7QO</scope><scope>7X8</scope><scope>7SC</scope><scope>7SP</scope><scope>7SR</scope><scope>7TB</scope><scope>7U5</scope><scope>8BQ</scope><scope>F28</scope><scope>JG9</scope><scope>JQ2</scope><scope>KR7</scope><scope>L7M</scope><scope>L~C</scope><scope>L~D</scope></search><sort><creationdate>19920206</creationdate><title>Selection of single-stranded DNA molecules that bind and inhibit human thrombin</title><author>Bock, Louis C ; 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1
are double-stranded DNA or single-stranded RNA molecules that bind specific molecular targets. Large randomly generated populations can be enriched in aptamers by
in vitro
selection and polymerase chain reaction
1–11
. But so far single-stranded DNA has not been investigated for aptamer properties, nor has a target protein been considered that does not interact physiologically with nucleic acid. Here we describe the isolation of single-stranded DNA aptamers to the protease thrombin of the blood coagulation cascade and report binding affinities in the range 25–200 nM. Sequence data from 32 thrsombin aptamers, selected from a pool of DNA containing 60 nucleotides of random sequence, displayed a highly conserved 14–17–base region. Several of these aptamers at nanomolar concentrations inhibited thrombin-catalysed fibrin-clot formation
in vitro
using either purified fibrinogen or human plasma.</abstract><cop>London</cop><pub>Nature Publishing Group UK</pub><pmid>1741036</pmid><doi>10.1038/355564a0</doi><tpages>3</tpages></addata></record> |
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| ispartof | Nature (London), 1992-02, Vol.355 (6360), p.564-566 |
| issn | 0028-0836 1476-4687 |
| language | eng |
| recordid | cdi_proquest_miscellaneous_743447442 |
| source | MEDLINE; SpringerLink Journals; Nature |
| subjects | Analytical, structural and metabolic biochemistry Base Sequence Biological and medical sciences Blood Blood Coagulation - drug effects Cloning, Molecular Coagulation Deoxyribonucleic acid DNA DNA, Single-Stranded - isolation & purification Dose-Response Relationship, Drug Enzymes and enzyme inhibitors Fundamental and applied biological sciences. Psychology Humanities and Social Sciences Humans Hydrolases In Vitro Techniques letter Medical research Molecular Sequence Data multidisciplinary Nucleic acids Polymerase Chain Reaction Science Science (multidisciplinary) Sequence Homology, Nucleic Acid Thrombin - antagonists & inhibitors Thrombin Time |
| title | Selection of single-stranded DNA molecules that bind and inhibit human thrombin |
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