Structural Determinants of Conformationally Selective, Prion-binding Aptamers[boxs]
We have recently described the isolation of 2′-fluoropyrimidine-substituted RNA aptamers that bind selectively to disease-associated β-sheet-rich forms of the prion protein, PrP, from a number of mammalian species. These aptamers inhibit the accumulation of protease-resistant forms of PrP in a prion...
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Veröffentlicht in: | The Journal of biological chemistry 2004-03, Vol.279 (13), p.13102-13109 |
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container_title | The Journal of biological chemistry |
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creator | Sayer, Natalie M. Cubin, Matthew Rhie, Alexandre Bullock, Marc Tahiri-Alaoui, Abdessamad James, William |
description | We have recently described the isolation of 2′-fluoropyrimidine-substituted RNA aptamers that bind selectively to disease-associated β-sheet-rich forms of the prion protein, PrP, from a number of mammalian species. These aptamers inhibit the accumulation of protease-resistant forms of PrP in a prion-seeded, in vitro conversion assay. Here we identify the minimal portions of two of these aptamers that retain binding specificity. We determine their secondary structures by a combination of modeling and solution probing. Finally, we identify an internal site for biotinylation of a minimized, synthetic aptamer and use the resultant reagent in the detection of abnormal forms of PrP in vitro. |
doi_str_mv | 10.1074/jbc.M310928200 |
format | Article |
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These aptamers inhibit the accumulation of protease-resistant forms of PrP in a prion-seeded, in vitro conversion assay. Here we identify the minimal portions of two of these aptamers that retain binding specificity. We determine their secondary structures by a combination of modeling and solution probing. Finally, we identify an internal site for biotinylation of a minimized, synthetic aptamer and use the resultant reagent in the detection of abnormal forms of PrP in vitro.</description><identifier>ISSN: 0021-9258</identifier><identifier>EISSN: 1083-351X</identifier><identifier>DOI: 10.1074/jbc.M310928200</identifier><identifier>PMID: 14711834</identifier><language>eng</language><publisher>United States: Elsevier Inc</publisher><subject>Animals ; Base Sequence ; Binding Sites ; Biotinylation ; Cattle ; Dose-Response Relationship, Drug ; Electrophoresis, Polyacrylamide Gel ; Escherichia coli - metabolism ; Kinetics ; Molecular Sequence Data ; Prions - chemistry ; Protein Binding ; Protein Conformation ; Protein Folding ; Protein Structure, Secondary ; RNA - chemistry ; Transcription, Genetic ; Urea - pharmacology</subject><ispartof>The Journal of biological chemistry, 2004-03, Vol.279 (13), p.13102-13109</ispartof><rights>2004 © 2004 ASBMB. 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These aptamers inhibit the accumulation of protease-resistant forms of PrP in a prion-seeded, in vitro conversion assay. Here we identify the minimal portions of two of these aptamers that retain binding specificity. We determine their secondary structures by a combination of modeling and solution probing. Finally, we identify an internal site for biotinylation of a minimized, synthetic aptamer and use the resultant reagent in the detection of abnormal forms of PrP in vitro.</description><subject>Animals</subject><subject>Base Sequence</subject><subject>Binding Sites</subject><subject>Biotinylation</subject><subject>Cattle</subject><subject>Dose-Response Relationship, Drug</subject><subject>Electrophoresis, Polyacrylamide Gel</subject><subject>Escherichia coli - metabolism</subject><subject>Kinetics</subject><subject>Molecular Sequence Data</subject><subject>Prions - chemistry</subject><subject>Protein Binding</subject><subject>Protein Conformation</subject><subject>Protein Folding</subject><subject>Protein Structure, Secondary</subject><subject>RNA - chemistry</subject><subject>Transcription, Genetic</subject><subject>Urea - pharmacology</subject><issn>0021-9258</issn><issn>1083-351X</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2004</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNp1kEtr20AQgJfSUDuPa49Fh5JT5MzotdIxOG0TcGjAKRRCWVarkb1G0jq7q6T-991gg08dBoYZvhmGj7HPCDMEnl1vajV7SBGqpEwAPrApQpnGaY6_P7IpQIJxleTlhJ06t4EQWYWf2AQzjlim2ZQtl96Oyo9WdtEtebK9HuTgXWTaaG6G1theem0G2XW7aEkdKa9f6Sp6tGEY13po9LCKbrZe9mTdc23-uj_n7KSVnaOLQz1jv75_e5rfxYufP-7nN4tY5VD4uC2AQPJMJQgNbyGpedrynCvK8qyWgMiLokUusSlUWaMs0opnaVnlAS5Dd8Yu93e31ryM5LzotVPUdXIgMzqBvALkwAM424PKGucstWJrdS_tTiCId40iaBRHjWHhy-HyWPfUHPGDtwB83QNrvVq_aUui1katqRcJrwSmIRGSgJV7jIKGV01WOKVpUNSEFeVFY_T_XvgHKJGMpA</recordid><startdate>20040326</startdate><enddate>20040326</enddate><creator>Sayer, Natalie M.</creator><creator>Cubin, Matthew</creator><creator>Rhie, Alexandre</creator><creator>Bullock, Marc</creator><creator>Tahiri-Alaoui, Abdessamad</creator><creator>James, William</creator><general>Elsevier Inc</general><general>American Society for Biochemistry and Molecular Biology</general><scope>6I.</scope><scope>AAFTH</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>7TM</scope><scope>7U9</scope><scope>H94</scope></search><sort><creationdate>20040326</creationdate><title>Structural Determinants of Conformationally Selective, Prion-binding Aptamers[boxs]</title><author>Sayer, Natalie M. ; Cubin, Matthew ; Rhie, Alexandre ; Bullock, Marc ; Tahiri-Alaoui, Abdessamad ; James, William</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c506t-f60e0a74c210d7f02b73f757ce454ba011766f17a1d6c8b1a6397438957f08a63</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2004</creationdate><topic>Animals</topic><topic>Base Sequence</topic><topic>Binding Sites</topic><topic>Biotinylation</topic><topic>Cattle</topic><topic>Dose-Response Relationship, Drug</topic><topic>Electrophoresis, Polyacrylamide Gel</topic><topic>Escherichia coli - metabolism</topic><topic>Kinetics</topic><topic>Molecular Sequence Data</topic><topic>Prions - chemistry</topic><topic>Protein Binding</topic><topic>Protein Conformation</topic><topic>Protein Folding</topic><topic>Protein Structure, Secondary</topic><topic>RNA - chemistry</topic><topic>Transcription, Genetic</topic><topic>Urea - pharmacology</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Sayer, Natalie M.</creatorcontrib><creatorcontrib>Cubin, Matthew</creatorcontrib><creatorcontrib>Rhie, Alexandre</creatorcontrib><creatorcontrib>Bullock, Marc</creatorcontrib><creatorcontrib>Tahiri-Alaoui, Abdessamad</creatorcontrib><creatorcontrib>James, William</creatorcontrib><collection>ScienceDirect Open Access Titles</collection><collection>Elsevier:ScienceDirect:Open Access</collection><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>Nucleic Acids Abstracts</collection><collection>Virology and AIDS Abstracts</collection><collection>AIDS and Cancer Research Abstracts</collection><jtitle>The Journal of biological chemistry</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Sayer, Natalie M.</au><au>Cubin, Matthew</au><au>Rhie, Alexandre</au><au>Bullock, Marc</au><au>Tahiri-Alaoui, Abdessamad</au><au>James, William</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Structural Determinants of Conformationally Selective, Prion-binding Aptamers[boxs]</atitle><jtitle>The Journal of biological chemistry</jtitle><addtitle>J Biol Chem</addtitle><date>2004-03-26</date><risdate>2004</risdate><volume>279</volume><issue>13</issue><spage>13102</spage><epage>13109</epage><pages>13102-13109</pages><issn>0021-9258</issn><eissn>1083-351X</eissn><abstract>We have recently described the isolation of 2′-fluoropyrimidine-substituted RNA aptamers that bind selectively to disease-associated β-sheet-rich forms of the prion protein, PrP, from a number of mammalian species. 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subjects | Animals Base Sequence Binding Sites Biotinylation Cattle Dose-Response Relationship, Drug Electrophoresis, Polyacrylamide Gel Escherichia coli - metabolism Kinetics Molecular Sequence Data Prions - chemistry Protein Binding Protein Conformation Protein Folding Protein Structure, Secondary RNA - chemistry Transcription, Genetic Urea - pharmacology |
title | Structural Determinants of Conformationally Selective, Prion-binding Aptamers[boxs] |
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