A dityrosine-based substrate for a protease assay: Application for the selective assessment of papain and chymopapain activity
[Display omitted] ► N,N′-diBoc-dityrosine (DBDY) was conjugated with two isoniazid (INH) molecules. ► Due to the quenching effect of INH, DBDY–(INH)2 lost the fluorescence of DBDY. ► Only papain and chymopapain catalyzed the hydrolysis of DBDY–(INH)2. ► DBDY–(INH)2 can be used as a selective and sen...
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| Veröffentlicht in: | Analytica chimica acta 2012-04, Vol.723, p.101-107 |
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| creator | Kim, Chan-Jin Lee, Dong-Ik Lee, Chang-Ha Ahn, Ik-Sung |
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► N,N′-diBoc-dityrosine (DBDY) was conjugated with two isoniazid (INH) molecules. ► Due to the quenching effect of INH, DBDY–(INH)2 lost the fluorescence of DBDY. ► Only papain and chymopapain catalyzed the hydrolysis of DBDY–(INH)2. ► DBDY–(INH)2 can be used as a selective and sensitive assay of papain and chymopapain.
N,N′-diBoc-dityrosine (DBDY), which was synthesized by the oxidative C–C coupling of 2 N-Boc-l-tyrosine molecules, was conjugated with two isoniazid (INH) molecules. Due to the quenching effect of INH, DBDY–(INH)2 lacks the fluorescence of DBDY. As such, it was tested for use in the detection of proteases by measuring fluorescence recovery. In this study, serine proteases (chymotrypsin, trypsin, subtilisin, and proteinase K), metalloproteases (thermolysin and carboxypeptidase A, dispase, and collagenase), aspartic proteases (pepsin and aspergillopepsin) and cysteine proteases (papain and chymopapain) were chosen. Reported optimum assay conditions were chosen for each enzyme. Only papain and chymopapain catalyzed the hydrolysis of DBDY–(INH)2 and led to fluorescence recovery, possibly due to their extensive binding sites and the INH-mediated inhibition of metalloproteases and aspartic proteases. |
| doi_str_mv | 10.1016/j.aca.2012.02.038 |
| format | Article |
| fullrecord | <record><control><sourceid>proquest_cross</sourceid><recordid>TN_cdi_proquest_miscellaneous_948906040</recordid><sourceformat>XML</sourceformat><sourcesystem>PC</sourcesystem><els_id>S0003267012003170</els_id><sourcerecordid>948906040</sourcerecordid><originalsourceid>FETCH-LOGICAL-c415t-cf8a2daf20eb014aabad4aeb785856bf24a84f4f760c9e1a7ec69a2fe6ce6de73</originalsourceid><addsrcrecordid>eNp90U1v1DAQBmALgei28AO4IF8QvWQZO47jwGlV8SVV4gJna-KMVa-ySbC9lfbCb8fb3cKt0kiW5cdf8zL2RsBagNAftmt0uJYg5BpK1eYZWwnT1pWqpXrOVgBQV1K3cMEuU9qWqRSgXrILKZVSjYEV-7PhQ8iHOKcwUdVjooGnfZ9yxEzcz5EjX-KcqaxwTAkPH_lmWcbgMId5ehD5jniikVwO9w-IUtrRlPns-YILhonjNHB3d9jNj_OjLfe-Yi88jolen8cr9uvL558336rbH1-_32xuK6dEkyvnDcoBvQTqQSjEHgeF1LemMY3uvVRolFe-1eA6EtiS0x1KT9qRHqitr9j707nlL7_3lLLdheRoHHGieZ9sp0wHGhQUef2kFCClMaZrjlScqCvtS5G8XWLYYTwUZI8B2a0tAdljQBZK1abseXs-ft_vaPi34zGRAt6dASaHo484uZD-u0brrgZd3KeTo9K2-0DRJhdocjSEWJKwwxyeeMZfbxCwoQ</addsrcrecordid><sourcetype>Aggregation Database</sourcetype><iscdi>true</iscdi><recordtype>article</recordtype><pqid>1022888950</pqid></control><display><type>article</type><title>A dityrosine-based substrate for a protease assay: Application for the selective assessment of papain and chymopapain activity</title><source>MEDLINE</source><source>Access via ScienceDirect (Elsevier)</source><creator>Kim, Chan-Jin ; Lee, Dong-Ik ; Lee, Chang-Ha ; Ahn, Ik-Sung</creator><creatorcontrib>Kim, Chan-Jin ; Lee, Dong-Ik ; Lee, Chang-Ha ; Ahn, Ik-Sung</creatorcontrib><description>[Display omitted]
► N,N′-diBoc-dityrosine (DBDY) was conjugated with two isoniazid (INH) molecules. ► Due to the quenching effect of INH, DBDY–(INH)2 lost the fluorescence of DBDY. ► Only papain and chymopapain catalyzed the hydrolysis of DBDY–(INH)2. ► DBDY–(INH)2 can be used as a selective and sensitive assay of papain and chymopapain.
N,N′-diBoc-dityrosine (DBDY), which was synthesized by the oxidative C–C coupling of 2 N-Boc-l-tyrosine molecules, was conjugated with two isoniazid (INH) molecules. Due to the quenching effect of INH, DBDY–(INH)2 lacks the fluorescence of DBDY. As such, it was tested for use in the detection of proteases by measuring fluorescence recovery. In this study, serine proteases (chymotrypsin, trypsin, subtilisin, and proteinase K), metalloproteases (thermolysin and carboxypeptidase A, dispase, and collagenase), aspartic proteases (pepsin and aspergillopepsin) and cysteine proteases (papain and chymopapain) were chosen. Reported optimum assay conditions were chosen for each enzyme. Only papain and chymopapain catalyzed the hydrolysis of DBDY–(INH)2 and led to fluorescence recovery, possibly due to their extensive binding sites and the INH-mediated inhibition of metalloproteases and aspartic proteases.</description><identifier>ISSN: 0003-2670</identifier><identifier>EISSN: 1873-4324</identifier><identifier>DOI: 10.1016/j.aca.2012.02.038</identifier><identifier>PMID: 22444580</identifier><identifier>CODEN: ACACAM</identifier><language>eng</language><publisher>Amsterdam: Elsevier B.V</publisher><subject>Analytical chemistry ; Assaying ; Assessments ; Biocatalysis ; Chemistry ; Chymopapain ; Chymopapain - metabolism ; Cysteine ; Dityrosine ; Enzyme Assays ; Enzymes ; Exact sciences and technology ; Fluorescence ; Hydrogen-Ion Concentration ; Hydrolysis ; Papain ; Papain - metabolism ; Protease ; Protease assay ; Recovery ; Spectrometric and optical methods ; Spectrometry, Fluorescence ; Substrate Specificity ; Temperature ; Tyrosine - analogs & derivatives ; Tyrosine - chemical synthesis ; Tyrosine - chemistry</subject><ispartof>Analytica chimica acta, 2012-04, Vol.723, p.101-107</ispartof><rights>2012 Elsevier B.V.</rights><rights>2015 INIST-CNRS</rights><rights>Copyright © 2012 Elsevier B.V. All rights reserved.</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c415t-cf8a2daf20eb014aabad4aeb785856bf24a84f4f760c9e1a7ec69a2fe6ce6de73</citedby><cites>FETCH-LOGICAL-c415t-cf8a2daf20eb014aabad4aeb785856bf24a84f4f760c9e1a7ec69a2fe6ce6de73</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktohtml>$$Uhttps://dx.doi.org/10.1016/j.aca.2012.02.038$$EHTML$$P50$$Gelsevier$$H</linktohtml><link.rule.ids>314,780,784,3550,27924,27925,45995</link.rule.ids><backlink>$$Uhttp://pascal-francis.inist.fr/vibad/index.php?action=getRecordDetail&idt=25669306$$DView record in Pascal Francis$$Hfree_for_read</backlink><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/22444580$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Kim, Chan-Jin</creatorcontrib><creatorcontrib>Lee, Dong-Ik</creatorcontrib><creatorcontrib>Lee, Chang-Ha</creatorcontrib><creatorcontrib>Ahn, Ik-Sung</creatorcontrib><title>A dityrosine-based substrate for a protease assay: Application for the selective assessment of papain and chymopapain activity</title><title>Analytica chimica acta</title><addtitle>Anal Chim Acta</addtitle><description>[Display omitted]
► N,N′-diBoc-dityrosine (DBDY) was conjugated with two isoniazid (INH) molecules. ► Due to the quenching effect of INH, DBDY–(INH)2 lost the fluorescence of DBDY. ► Only papain and chymopapain catalyzed the hydrolysis of DBDY–(INH)2. ► DBDY–(INH)2 can be used as a selective and sensitive assay of papain and chymopapain.
N,N′-diBoc-dityrosine (DBDY), which was synthesized by the oxidative C–C coupling of 2 N-Boc-l-tyrosine molecules, was conjugated with two isoniazid (INH) molecules. Due to the quenching effect of INH, DBDY–(INH)2 lacks the fluorescence of DBDY. As such, it was tested for use in the detection of proteases by measuring fluorescence recovery. In this study, serine proteases (chymotrypsin, trypsin, subtilisin, and proteinase K), metalloproteases (thermolysin and carboxypeptidase A, dispase, and collagenase), aspartic proteases (pepsin and aspergillopepsin) and cysteine proteases (papain and chymopapain) were chosen. Reported optimum assay conditions were chosen for each enzyme. Only papain and chymopapain catalyzed the hydrolysis of DBDY–(INH)2 and led to fluorescence recovery, possibly due to their extensive binding sites and the INH-mediated inhibition of metalloproteases and aspartic proteases.</description><subject>Analytical chemistry</subject><subject>Assaying</subject><subject>Assessments</subject><subject>Biocatalysis</subject><subject>Chemistry</subject><subject>Chymopapain</subject><subject>Chymopapain - metabolism</subject><subject>Cysteine</subject><subject>Dityrosine</subject><subject>Enzyme Assays</subject><subject>Enzymes</subject><subject>Exact sciences and technology</subject><subject>Fluorescence</subject><subject>Hydrogen-Ion Concentration</subject><subject>Hydrolysis</subject><subject>Papain</subject><subject>Papain - metabolism</subject><subject>Protease</subject><subject>Protease assay</subject><subject>Recovery</subject><subject>Spectrometric and optical methods</subject><subject>Spectrometry, Fluorescence</subject><subject>Substrate Specificity</subject><subject>Temperature</subject><subject>Tyrosine - analogs & derivatives</subject><subject>Tyrosine - chemical synthesis</subject><subject>Tyrosine - chemistry</subject><issn>0003-2670</issn><issn>1873-4324</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2012</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNp90U1v1DAQBmALgei28AO4IF8QvWQZO47jwGlV8SVV4gJna-KMVa-ySbC9lfbCb8fb3cKt0kiW5cdf8zL2RsBagNAftmt0uJYg5BpK1eYZWwnT1pWqpXrOVgBQV1K3cMEuU9qWqRSgXrILKZVSjYEV-7PhQ8iHOKcwUdVjooGnfZ9yxEzcz5EjX-KcqaxwTAkPH_lmWcbgMId5ehD5jniikVwO9w-IUtrRlPns-YILhonjNHB3d9jNj_OjLfe-Yi88jolen8cr9uvL558336rbH1-_32xuK6dEkyvnDcoBvQTqQSjEHgeF1LemMY3uvVRolFe-1eA6EtiS0x1KT9qRHqitr9j707nlL7_3lLLdheRoHHGieZ9sp0wHGhQUef2kFCClMaZrjlScqCvtS5G8XWLYYTwUZI8B2a0tAdljQBZK1abseXs-ft_vaPi34zGRAt6dASaHo484uZD-u0brrgZd3KeTo9K2-0DRJhdocjSEWJKwwxyeeMZfbxCwoQ</recordid><startdate>20120420</startdate><enddate>20120420</enddate><creator>Kim, Chan-Jin</creator><creator>Lee, Dong-Ik</creator><creator>Lee, Chang-Ha</creator><creator>Ahn, Ik-Sung</creator><general>Elsevier B.V</general><general>Elsevier</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>7U5</scope><scope>8FD</scope><scope>L7M</scope><scope>7X8</scope></search><sort><creationdate>20120420</creationdate><title>A dityrosine-based substrate for a protease assay: Application for the selective assessment of papain and chymopapain activity</title><author>Kim, Chan-Jin ; Lee, Dong-Ik ; Lee, Chang-Ha ; Ahn, Ik-Sung</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c415t-cf8a2daf20eb014aabad4aeb785856bf24a84f4f760c9e1a7ec69a2fe6ce6de73</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2012</creationdate><topic>Analytical chemistry</topic><topic>Assaying</topic><topic>Assessments</topic><topic>Biocatalysis</topic><topic>Chemistry</topic><topic>Chymopapain</topic><topic>Chymopapain - metabolism</topic><topic>Cysteine</topic><topic>Dityrosine</topic><topic>Enzyme Assays</topic><topic>Enzymes</topic><topic>Exact sciences and technology</topic><topic>Fluorescence</topic><topic>Hydrogen-Ion Concentration</topic><topic>Hydrolysis</topic><topic>Papain</topic><topic>Papain - metabolism</topic><topic>Protease</topic><topic>Protease assay</topic><topic>Recovery</topic><topic>Spectrometric and optical methods</topic><topic>Spectrometry, Fluorescence</topic><topic>Substrate Specificity</topic><topic>Temperature</topic><topic>Tyrosine - analogs & derivatives</topic><topic>Tyrosine - chemical synthesis</topic><topic>Tyrosine - chemistry</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Kim, Chan-Jin</creatorcontrib><creatorcontrib>Lee, Dong-Ik</creatorcontrib><creatorcontrib>Lee, Chang-Ha</creatorcontrib><creatorcontrib>Ahn, Ik-Sung</creatorcontrib><collection>Pascal-Francis</collection><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>Solid State and Superconductivity Abstracts</collection><collection>Technology Research Database</collection><collection>Advanced Technologies Database with Aerospace</collection><collection>MEDLINE - Academic</collection><jtitle>Analytica chimica acta</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Kim, Chan-Jin</au><au>Lee, Dong-Ik</au><au>Lee, Chang-Ha</au><au>Ahn, Ik-Sung</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>A dityrosine-based substrate for a protease assay: Application for the selective assessment of papain and chymopapain activity</atitle><jtitle>Analytica chimica acta</jtitle><addtitle>Anal Chim Acta</addtitle><date>2012-04-20</date><risdate>2012</risdate><volume>723</volume><spage>101</spage><epage>107</epage><pages>101-107</pages><issn>0003-2670</issn><eissn>1873-4324</eissn><coden>ACACAM</coden><abstract>[Display omitted]
► N,N′-diBoc-dityrosine (DBDY) was conjugated with two isoniazid (INH) molecules. ► Due to the quenching effect of INH, DBDY–(INH)2 lost the fluorescence of DBDY. ► Only papain and chymopapain catalyzed the hydrolysis of DBDY–(INH)2. ► DBDY–(INH)2 can be used as a selective and sensitive assay of papain and chymopapain.
N,N′-diBoc-dityrosine (DBDY), which was synthesized by the oxidative C–C coupling of 2 N-Boc-l-tyrosine molecules, was conjugated with two isoniazid (INH) molecules. Due to the quenching effect of INH, DBDY–(INH)2 lacks the fluorescence of DBDY. As such, it was tested for use in the detection of proteases by measuring fluorescence recovery. In this study, serine proteases (chymotrypsin, trypsin, subtilisin, and proteinase K), metalloproteases (thermolysin and carboxypeptidase A, dispase, and collagenase), aspartic proteases (pepsin and aspergillopepsin) and cysteine proteases (papain and chymopapain) were chosen. Reported optimum assay conditions were chosen for each enzyme. Only papain and chymopapain catalyzed the hydrolysis of DBDY–(INH)2 and led to fluorescence recovery, possibly due to their extensive binding sites and the INH-mediated inhibition of metalloproteases and aspartic proteases.</abstract><cop>Amsterdam</cop><pub>Elsevier B.V</pub><pmid>22444580</pmid><doi>10.1016/j.aca.2012.02.038</doi><tpages>7</tpages></addata></record> |
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| subjects | Analytical chemistry Assaying Assessments Biocatalysis Chemistry Chymopapain Chymopapain - metabolism Cysteine Dityrosine Enzyme Assays Enzymes Exact sciences and technology Fluorescence Hydrogen-Ion Concentration Hydrolysis Papain Papain - metabolism Protease Protease assay Recovery Spectrometric and optical methods Spectrometry, Fluorescence Substrate Specificity Temperature Tyrosine - analogs & derivatives Tyrosine - chemical synthesis Tyrosine - chemistry |
| title | A dityrosine-based substrate for a protease assay: Application for the selective assessment of papain and chymopapain activity |
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