Structure-based design of a fluorimetric redox active peptide probe
Structure-based iterative design was used to prepare a disulfide-containing nonapeptide as a fluorimetric probe for chemical and biochemical disulfide forming and breaking reactions. The peptide is composed entirely of natural amino acids and exhibits a marked (42%) change in fluorescence between it...
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| Veröffentlicht in: | Analytical biochemistry 2004-02, Vol.325 (1), p.144-150 |
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| creator | Cline, Daniel J. Thorpe, Colin Schneider, Joel P. |
| description | Structure-based iterative design was used to prepare a disulfide-containing nonapeptide as a fluorimetric probe for chemical and biochemical disulfide forming and breaking reactions. The peptide is composed entirely of natural amino acids and exhibits a marked (42%) change in fluorescence between its oxidized and its reduced states. The probe is easily synthesized and highly water soluble and exhibits well-behaved kinetics on reduction with the reductant tris–carboxyethylphosphine. The reduced peptide is an excellent substrate of the enzyme quiescin–sulfhydryl oxidase and may find utility in the characterization of other disulfide oxidoreductases. |
| doi_str_mv | 10.1016/j.ab.2003.10.014 |
| format | Article |
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The peptide is composed entirely of natural amino acids and exhibits a marked (42%) change in fluorescence between its oxidized and its reduced states. The probe is easily synthesized and highly water soluble and exhibits well-behaved kinetics on reduction with the reductant tris–carboxyethylphosphine. The reduced peptide is an excellent substrate of the enzyme quiescin–sulfhydryl oxidase and may find utility in the characterization of other disulfide oxidoreductases.</description><identifier>ISSN: 0003-2697</identifier><identifier>EISSN: 1096-0309</identifier><identifier>DOI: 10.1016/j.ab.2003.10.014</identifier><identifier>PMID: 14715295</identifier><language>eng</language><publisher>United States: Elsevier Inc</publisher><subject>Amino Acid Sequence ; Fluorescent Dyes - chemical synthesis ; Fluorescent Dyes - chemistry ; Humans ; Magnetic Resonance Spectroscopy ; Molecular Structure ; Oxidation-Reduction ; Oxidoreductases - chemistry ; Peptides - chemical synthesis ; Peptides - chemistry ; Peptides - pharmacology ; Spectrometry, Fluorescence ; Thioredoxins - chemistry</subject><ispartof>Analytical biochemistry, 2004-02, Vol.325 (1), p.144-150</ispartof><rights>2003 Elsevier Inc.</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c412t-1f0455e2464d96d5045da2a4dec13445abd53fbad6c7842c32a61afc2930ae5b3</citedby><cites>FETCH-LOGICAL-c412t-1f0455e2464d96d5045da2a4dec13445abd53fbad6c7842c32a61afc2930ae5b3</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktohtml>$$Uhttps://dx.doi.org/10.1016/j.ab.2003.10.014$$EHTML$$P50$$Gelsevier$$H</linktohtml><link.rule.ids>314,780,784,3550,27924,27925,45995</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/14715295$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Cline, Daniel J.</creatorcontrib><creatorcontrib>Thorpe, Colin</creatorcontrib><creatorcontrib>Schneider, Joel P.</creatorcontrib><title>Structure-based design of a fluorimetric redox active peptide probe</title><title>Analytical biochemistry</title><addtitle>Anal Biochem</addtitle><description>Structure-based iterative design was used to prepare a disulfide-containing nonapeptide as a fluorimetric probe for chemical and biochemical disulfide forming and breaking reactions. The peptide is composed entirely of natural amino acids and exhibits a marked (42%) change in fluorescence between its oxidized and its reduced states. The probe is easily synthesized and highly water soluble and exhibits well-behaved kinetics on reduction with the reductant tris–carboxyethylphosphine. The reduced peptide is an excellent substrate of the enzyme quiescin–sulfhydryl oxidase and may find utility in the characterization of other disulfide oxidoreductases.</description><subject>Amino Acid Sequence</subject><subject>Fluorescent Dyes - chemical synthesis</subject><subject>Fluorescent Dyes - chemistry</subject><subject>Humans</subject><subject>Magnetic Resonance Spectroscopy</subject><subject>Molecular Structure</subject><subject>Oxidation-Reduction</subject><subject>Oxidoreductases - chemistry</subject><subject>Peptides - chemical synthesis</subject><subject>Peptides - chemistry</subject><subject>Peptides - pharmacology</subject><subject>Spectrometry, Fluorescence</subject><subject>Thioredoxins - chemistry</subject><issn>0003-2697</issn><issn>1096-0309</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2004</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNp1UE1LAzEUDKLYWr17kj152_Ulm6Rdb1LqBxQ8qOeQj7eSsu3WJFv035vSgidPj3lvZh4zhFxTqChQebeqtKkYQJ1hBZSfkDGFRpZQQ3NKxpAvJZPNdEQuYlwBUMqFPCcjyqdUsEaMyfwthcGmIWBpdERXOIz-c1P0baGLthv64NeYgrdFQNd_F9omv8Nii9vkXZ6hN3hJzlrdRbw6zgn5eFy8z5_L5evTy_xhWVpOWSppC1wIZFxy10gnMnKaae7Q0ppzoY0TdWu0k3Y648zWTEuqW8uaGjQKU0_I7cE3f_0aMCa19tFi1-kN9kNUM4BGMDHLRDgQbehjDNiqbY6hw4-ioPbFqZXSRu2L229ycVlyc_QezBrdn-DYVCbcHwiYE-48BhWtx41F5wPapFzv_3f_BYRbfQE</recordid><startdate>20040201</startdate><enddate>20040201</enddate><creator>Cline, Daniel J.</creator><creator>Thorpe, Colin</creator><creator>Schneider, Joel P.</creator><general>Elsevier Inc</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>7X8</scope></search><sort><creationdate>20040201</creationdate><title>Structure-based design of a fluorimetric redox active peptide probe</title><author>Cline, Daniel J. ; Thorpe, Colin ; Schneider, Joel P.</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c412t-1f0455e2464d96d5045da2a4dec13445abd53fbad6c7842c32a61afc2930ae5b3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2004</creationdate><topic>Amino Acid Sequence</topic><topic>Fluorescent Dyes - chemical synthesis</topic><topic>Fluorescent Dyes - chemistry</topic><topic>Humans</topic><topic>Magnetic Resonance Spectroscopy</topic><topic>Molecular Structure</topic><topic>Oxidation-Reduction</topic><topic>Oxidoreductases - chemistry</topic><topic>Peptides - chemical synthesis</topic><topic>Peptides - chemistry</topic><topic>Peptides - pharmacology</topic><topic>Spectrometry, Fluorescence</topic><topic>Thioredoxins - chemistry</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Cline, Daniel J.</creatorcontrib><creatorcontrib>Thorpe, Colin</creatorcontrib><creatorcontrib>Schneider, Joel P.</creatorcontrib><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>MEDLINE - Academic</collection><jtitle>Analytical biochemistry</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Cline, Daniel J.</au><au>Thorpe, Colin</au><au>Schneider, Joel P.</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Structure-based design of a fluorimetric redox active peptide probe</atitle><jtitle>Analytical biochemistry</jtitle><addtitle>Anal Biochem</addtitle><date>2004-02-01</date><risdate>2004</risdate><volume>325</volume><issue>1</issue><spage>144</spage><epage>150</epage><pages>144-150</pages><issn>0003-2697</issn><eissn>1096-0309</eissn><abstract>Structure-based iterative design was used to prepare a disulfide-containing nonapeptide as a fluorimetric probe for chemical and biochemical disulfide forming and breaking reactions. The peptide is composed entirely of natural amino acids and exhibits a marked (42%) change in fluorescence between its oxidized and its reduced states. The probe is easily synthesized and highly water soluble and exhibits well-behaved kinetics on reduction with the reductant tris–carboxyethylphosphine. The reduced peptide is an excellent substrate of the enzyme quiescin–sulfhydryl oxidase and may find utility in the characterization of other disulfide oxidoreductases.</abstract><cop>United States</cop><pub>Elsevier Inc</pub><pmid>14715295</pmid><doi>10.1016/j.ab.2003.10.014</doi><tpages>7</tpages></addata></record> |
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| ispartof | Analytical biochemistry, 2004-02, Vol.325 (1), p.144-150 |
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| source | MEDLINE; Access via ScienceDirect (Elsevier) |
| subjects | Amino Acid Sequence Fluorescent Dyes - chemical synthesis Fluorescent Dyes - chemistry Humans Magnetic Resonance Spectroscopy Molecular Structure Oxidation-Reduction Oxidoreductases - chemistry Peptides - chemical synthesis Peptides - chemistry Peptides - pharmacology Spectrometry, Fluorescence Thioredoxins - chemistry |
| title | Structure-based design of a fluorimetric redox active peptide probe |
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