A miniaturized peptidyl-prolyl isomerase enzyme assay.
Identifieur interne : 001307 ( PubMed/Checkpoint ); précédent : 001306; suivant : 001308A miniaturized peptidyl-prolyl isomerase enzyme assay.
Auteurs : Mirella Vivoli [Royaume-Uni] ; Julien Renou [France] ; Arnaud Chevalier [France] ; Isobel H. Norville [Royaume-Uni] ; Suraya Diaz [Royaume-Uni] ; Christina Juli [Allemagne] ; Helen Atkins [Royaume-Uni] ; Ulrike Holzgrabe [Allemagne] ; Pierre-Yves Renard [France] ; Mitali Sarkar-Tyson [Australie] ; Nicholas J. Harmer [Royaume-Uni]Source :
- Analytical biochemistry [ 1096-0309 ] ; 2017.
Abstract
Prolyl-peptidyl isomerases (PPIases) are enzymes that are found in all living organisms. They form an essential part of the cellular protein folding homeostasis machinery. PPIases are associated with many important human diseases, e.g. cardiovascular disease, cancer and Alzheimer's. The development of novel PPIase inhibitors has been limited by the lack of a rapid, laboratory-based assay for these enzymes, as their substrates and products are challenging to distinguish. A well described continuous assay, coupled with the hydrolysis of a peptide by chymotrypsin is highly effective, but comparatively slow. To address this, we developed an improved version of the traditional assay using a temperature controlled plate reader. This assay allows semi-automated medium throughput assays in an academic laboratory for 84 samples per day. The assay shows lower errors, with an average Z' of 0.72. We further developed the assay using a fluorogenic peptide-based FRET probe. This provides an extremely sensitive PPIase assay using substrate at 200 nM, which approaches single turnover conditions. The fluorescent probe achieves an excellent quenching efficiency of 98.6%, and initial experiments showed acceptable Z' of 0.31 and 0.30 for cyclophilin A and hFKBP12 respectively. The assays provide an improved toolset for the quantitative, biochemical analysis of PPIases.
DOI: 10.1016/j.ab.2017.08.004
PubMed: 28803887
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Norville</name><affiliation wicri:level="1"><nlm:affiliation>Defence Science and Technology Laboratory, Porton Down SP4 0JQ, United Kingdom.</nlm:affiliation><country xml:lang="fr">Royaume-Uni</country><wicri:regionArea>Defence Science and Technology Laboratory, Porton Down SP4 0JQ</wicri:regionArea><wicri:noRegion>Porton Down SP4 0JQ</wicri:noRegion></affiliation></author><author><name sortKey="Diaz, Suraya" sort="Diaz, Suraya" uniqKey="Diaz S" first="Suraya" last="Diaz">Suraya Diaz</name><affiliation wicri:level="1"><nlm:affiliation>College of Life and Environmental Sciences, University of Exeter, Exeter EX4 4QD, United Kingdom.</nlm:affiliation><country xml:lang="fr">Royaume-Uni</country><wicri:regionArea>College of Life and Environmental Sciences, University of Exeter, Exeter EX4 4QD</wicri:regionArea><wicri:noRegion>Exeter EX4 4QD</wicri:noRegion></affiliation></author><author><name sortKey="Juli, Christina" sort="Juli, Christina" uniqKey="Juli C" first="Christina" last="Juli">Christina Juli</name><affiliation wicri:level="1"><nlm:affiliation>Institute of Pharmacy, University of Würzburg, Am Hubland, 970074 Würzburg, Germany.</nlm:affiliation><country xml:lang="fr">Allemagne</country><wicri:regionArea>Institute of Pharmacy, University of Würzburg, Am Hubland, 970074 Würzburg</wicri:regionArea><wicri:noRegion>970074 Würzburg</wicri:noRegion><wicri:noRegion>970074 Würzburg</wicri:noRegion><wicri:noRegion>970074 Würzburg</wicri:noRegion></affiliation></author><author><name sortKey="Atkins, Helen" sort="Atkins, Helen" uniqKey="Atkins H" first="Helen" last="Atkins">Helen Atkins</name><affiliation wicri:level="1"><nlm:affiliation>Defence Science and Technology Laboratory, Porton Down SP4 0JQ, United Kingdom.</nlm:affiliation><country xml:lang="fr">Royaume-Uni</country><wicri:regionArea>Defence Science and Technology Laboratory, Porton Down SP4 0JQ</wicri:regionArea><wicri:noRegion>Porton Down SP4 0JQ</wicri:noRegion></affiliation></author><author><name sortKey="Holzgrabe, Ulrike" sort="Holzgrabe, Ulrike" uniqKey="Holzgrabe U" first="Ulrike" last="Holzgrabe">Ulrike Holzgrabe</name><affiliation wicri:level="1"><nlm:affiliation>Institute of Pharmacy, University of Würzburg, Am Hubland, 970074 Würzburg, Germany.</nlm:affiliation><country xml:lang="fr">Allemagne</country><wicri:regionArea>Institute of Pharmacy, University of Würzburg, Am Hubland, 970074 Würzburg</wicri:regionArea><wicri:noRegion>970074 Würzburg</wicri:noRegion><wicri:noRegion>970074 Würzburg</wicri:noRegion><wicri:noRegion>970074 Würzburg</wicri:noRegion></affiliation></author><author><name sortKey="Renard, Pierre Yves" sort="Renard, Pierre Yves" uniqKey="Renard P" first="Pierre-Yves" last="Renard">Pierre-Yves Renard</name><affiliation wicri:level="1"><nlm:affiliation>Normandie Univ, UNIROUEN, CNRS, INSAREOUEN, COBRA, UMR 6014 & FR 3038, 1 rue Tesnière 76000 Rouen, France.</nlm:affiliation><country xml:lang="fr">France</country><wicri:regionArea>Normandie Univ, UNIROUEN, CNRS, INSAREOUEN, COBRA, UMR 6014 & FR 3038, 1 rue Tesnière 76000 Rouen</wicri:regionArea><wicri:noRegion>76000 Rouen</wicri:noRegion><wicri:noRegion>76000 Rouen</wicri:noRegion></affiliation></author><author><name sortKey="Sarkar Tyson, Mitali" sort="Sarkar Tyson, Mitali" uniqKey="Sarkar Tyson M" first="Mitali" last="Sarkar-Tyson">Mitali Sarkar-Tyson</name><affiliation wicri:level="1"><nlm:affiliation>Defence Science and Technology Laboratory, Porton Down SP4 0JQ, United Kingdom; Marshall Centre for Infectious Diseases, School of Pathology and Laboratory Medicine, University of Western Australia, Crawley, WA 6009, Australia.</nlm:affiliation><country xml:lang="fr">Australie</country><wicri:regionArea>Defence Science and Technology Laboratory, Porton Down SP4 0JQ, United Kingdom; Marshall Centre for Infectious Diseases, School of Pathology and Laboratory Medicine, University of Western Australia, Crawley, WA 6009</wicri:regionArea><wicri:noRegion>WA 6009</wicri:noRegion></affiliation></author><author><name sortKey="Harmer, Nicholas J" sort="Harmer, Nicholas J" uniqKey="Harmer N" first="Nicholas J" last="Harmer">Nicholas J. Harmer</name><affiliation wicri:level="1"><nlm:affiliation>College of Life and Environmental Sciences, University of Exeter, Exeter EX4 4QD, United Kingdom. Electronic address: N.J.Harmer@exeter.ac.uk.</nlm:affiliation><country xml:lang="fr">Royaume-Uni</country><wicri:regionArea>College of Life and Environmental Sciences, University of Exeter, Exeter EX4 4QD</wicri:regionArea><wicri:noRegion>Exeter EX4 4QD</wicri:noRegion></affiliation></author></analytic><series><title level="j">Analytical biochemistry</title><idno type="eISSN">1096-0309</idno><imprint><date when="2017" type="published">2017</date></imprint></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">Prolyl-peptidyl isomerases (PPIases) are enzymes that are found in all living organisms. They form an essential part of the cellular protein folding homeostasis machinery. PPIases are associated with many important human diseases, e.g. cardiovascular disease, cancer and Alzheimer's. The development of novel PPIase inhibitors has been limited by the lack of a rapid, laboratory-based assay for these enzymes, as their substrates and products are challenging to distinguish. A well described continuous assay, coupled with the hydrolysis of a peptide by chymotrypsin is highly effective, but comparatively slow. To address this, we developed an improved version of the traditional assay using a temperature controlled plate reader. This assay allows semi-automated medium throughput assays in an academic laboratory for 84 samples per day. The assay shows lower errors, with an average Z' of 0.72. We further developed the assay using a fluorogenic peptide-based FRET probe. This provides an extremely sensitive PPIase assay using substrate at 200 nM, which approaches single turnover conditions. The fluorescent probe achieves an excellent quenching efficiency of 98.6%, and initial experiments showed acceptable Z' of 0.31 and 0.30 for cyclophilin A and hFKBP12 respectively. The assays provide an improved toolset for the quantitative, biochemical analysis of PPIases.</div></front></TEI><pubmed><MedlineCitation Status="Publisher" Owner="NLM"><PMID Version="1">28803887</PMID><DateCreated><Year>2017</Year><Month>08</Month><Day>14</Day></DateCreated><DateRevised><Year>2017</Year><Month>11</Month><Day>10</Day></DateRevised><Article PubModel="Print-Electronic"><Journal><ISSN IssnType="Electronic">1096-0309</ISSN><JournalIssue CitedMedium="Internet"><Volume>536</Volume><PubDate><Year>2017</Year><Month>Aug</Month><Day>11</Day></PubDate></JournalIssue><Title>Analytical biochemistry</Title><ISOAbbreviation>Anal. Biochem.</ISOAbbreviation></Journal><ArticleTitle>A miniaturized peptidyl-prolyl isomerase enzyme assay.</ArticleTitle><Pagination><MedlinePgn>59-68</MedlinePgn></Pagination><ELocationID EIdType="pii" ValidYN="Y">S0003-2697(17)30336-6</ELocationID><ELocationID EIdType="doi" ValidYN="Y">10.1016/j.ab.2017.08.004</ELocationID><Abstract><AbstractText>Prolyl-peptidyl isomerases (PPIases) are enzymes that are found in all living organisms. They form an essential part of the cellular protein folding homeostasis machinery. PPIases are associated with many important human diseases, e.g. cardiovascular disease, cancer and Alzheimer's. The development of novel PPIase inhibitors has been limited by the lack of a rapid, laboratory-based assay for these enzymes, as their substrates and products are challenging to distinguish. A well described continuous assay, coupled with the hydrolysis of a peptide by chymotrypsin is highly effective, but comparatively slow. To address this, we developed an improved version of the traditional assay using a temperature controlled plate reader. This assay allows semi-automated medium throughput assays in an academic laboratory for 84 samples per day. The assay shows lower errors, with an average Z' of 0.72. We further developed the assay using a fluorogenic peptide-based FRET probe. This provides an extremely sensitive PPIase assay using substrate at 200 nM, which approaches single turnover conditions. The fluorescent probe achieves an excellent quenching efficiency of 98.6%, and initial experiments showed acceptable Z' of 0.31 and 0.30 for cyclophilin A and hFKBP12 respectively. The assays provide an improved toolset for the quantitative, biochemical analysis of PPIases.</AbstractText><CopyrightInformation>Crown Copyright © 2017. Published by Elsevier Inc. All rights reserved.</CopyrightInformation></Abstract><AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Vivoli</LastName><ForeName>Mirella</ForeName><Initials>M</Initials><AffiliationInfo><Affiliation>College of Life and Environmental Sciences, University of Exeter, Exeter EX4 4QD, United Kingdom.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Renou</LastName><ForeName>Julien</ForeName><Initials>J</Initials><AffiliationInfo><Affiliation>Normandie Univ, UNIROUEN, CNRS, INSAREOUEN, COBRA, UMR 6014 & FR 3038, 1 rue Tesnière 76000 Rouen, France.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Chevalier</LastName><ForeName>Arnaud</ForeName><Initials>A</Initials><AffiliationInfo><Affiliation>Normandie Univ, UNIROUEN, CNRS, INSAREOUEN, COBRA, UMR 6014 & FR 3038, 1 rue Tesnière 76000 Rouen, France.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Norville</LastName><ForeName>Isobel H</ForeName><Initials>IH</Initials><AffiliationInfo><Affiliation>Defence Science and Technology Laboratory, Porton Down SP4 0JQ, United Kingdom.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Diaz</LastName><ForeName>Suraya</ForeName><Initials>S</Initials><AffiliationInfo><Affiliation>College of Life and Environmental Sciences, University of Exeter, Exeter EX4 4QD, United Kingdom.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Juli</LastName><ForeName>Christina</ForeName><Initials>C</Initials><AffiliationInfo><Affiliation>Institute of Pharmacy, University of Würzburg, Am Hubland, 970074 Würzburg, Germany.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Atkins</LastName><ForeName>Helen</ForeName><Initials>H</Initials><AffiliationInfo><Affiliation>Defence Science and Technology Laboratory, Porton Down SP4 0JQ, United Kingdom.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Holzgrabe</LastName><ForeName>Ulrike</ForeName><Initials>U</Initials><AffiliationInfo><Affiliation>Institute of Pharmacy, University of Würzburg, Am Hubland, 970074 Würzburg, Germany.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Renard</LastName><ForeName>Pierre-Yves</ForeName><Initials>PY</Initials><AffiliationInfo><Affiliation>Normandie Univ, UNIROUEN, CNRS, INSAREOUEN, COBRA, UMR 6014 & FR 3038, 1 rue Tesnière 76000 Rouen, France.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Sarkar-Tyson</LastName><ForeName>Mitali</ForeName><Initials>M</Initials><AffiliationInfo><Affiliation>Defence Science and Technology Laboratory, Porton Down SP4 0JQ, United Kingdom; Marshall Centre for Infectious Diseases, School of Pathology and Laboratory Medicine, University of Western Australia, Crawley, WA 6009, Australia.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Harmer</LastName><ForeName>Nicholas J</ForeName><Initials>NJ</Initials><AffiliationInfo><Affiliation>College of Life and Environmental Sciences, University of Exeter, Exeter EX4 4QD, United Kingdom. Electronic address: N.J.Harmer@exeter.ac.uk.</Affiliation></AffiliationInfo></Author></AuthorList><Language>eng</Language><PublicationTypeList><PublicationType UI="D016428">Journal Article</PublicationType></PublicationTypeList><ArticleDate DateType="Electronic"><Year>2017</Year><Month>08</Month><Day>11</Day></ArticleDate></Article><MedlineJournalInfo><Country>United States</Country><MedlineTA>Anal Biochem</MedlineTA><NlmUniqueID>0370535</NlmUniqueID><ISSNLinking>0003-2697</ISSNLinking></MedlineJournalInfo><KeywordList Owner="NOTNLM"><Keyword MajorTopicYN="N">Assay development</Keyword><Keyword MajorTopicYN="N">Cyclophilin</Keyword><Keyword MajorTopicYN="N">FKBP12</Keyword><Keyword MajorTopicYN="N">Fluorescence</Keyword><Keyword MajorTopicYN="N">High throughput</Keyword><Keyword MajorTopicYN="N">Inhibitor</Keyword><Keyword MajorTopicYN="N">Peptide</Keyword></KeywordList></MedlineCitation><PubmedData><History><PubMedPubDate PubStatus="received"><Year>2017</Year><Month>02</Month><Day>14</Day></PubMedPubDate><PubMedPubDate PubStatus="revised"><Year>2017</Year><Month>08</Month><Day>04</Day></PubMedPubDate><PubMedPubDate PubStatus="accepted"><Year>2017</Year><Month>08</Month><Day>09</Day></PubMedPubDate><PubMedPubDate PubStatus="pubmed"><Year>2017</Year><Month>8</Month><Day>15</Day><Hour>6</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate PubStatus="medline"><Year>2017</Year><Month>8</Month><Day>15</Day><Hour>6</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate PubStatus="entrez"><Year>2017</Year><Month>8</Month><Day>15</Day><Hour>6</Hour><Minute>0</Minute></PubMedPubDate></History><PublicationStatus>aheadofprint</PublicationStatus><ArticleIdList><ArticleId IdType="pubmed">28803887</ArticleId><ArticleId IdType="pii">S0003-2697(17)30336-6</ArticleId><ArticleId IdType="doi">10.1016/j.ab.2017.08.004</ArticleId></ArticleIdList></PubmedData></pubmed><affiliations><list><country><li>Allemagne</li><li>Australie</li><li>France</li><li>Royaume-Uni</li></country></list><tree><country name="Royaume-Uni"><noRegion><name sortKey="Vivoli, Mirella" sort="Vivoli, Mirella" uniqKey="Vivoli M" first="Mirella" last="Vivoli">Mirella Vivoli</name></noRegion><name sortKey="Atkins, Helen" sort="Atkins, Helen" uniqKey="Atkins H" first="Helen" last="Atkins">Helen Atkins</name><name sortKey="Diaz, Suraya" sort="Diaz, Suraya" uniqKey="Diaz S" first="Suraya" last="Diaz">Suraya Diaz</name><name sortKey="Harmer, Nicholas J" sort="Harmer, Nicholas J" uniqKey="Harmer N" first="Nicholas J" last="Harmer">Nicholas J. Harmer</name><name sortKey="Norville, Isobel H" sort="Norville, Isobel H" uniqKey="Norville I" first="Isobel H" last="Norville">Isobel H. Norville</name></country><country name="France"><noRegion><name sortKey="Renou, Julien" sort="Renou, Julien" uniqKey="Renou J" first="Julien" last="Renou">Julien Renou</name></noRegion><name sortKey="Chevalier, Arnaud" sort="Chevalier, Arnaud" uniqKey="Chevalier A" first="Arnaud" last="Chevalier">Arnaud Chevalier</name><name sortKey="Renard, Pierre Yves" sort="Renard, Pierre Yves" uniqKey="Renard P" first="Pierre-Yves" last="Renard">Pierre-Yves Renard</name></country><country name="Allemagne"><noRegion><name sortKey="Juli, Christina" sort="Juli, Christina" uniqKey="Juli C" first="Christina" last="Juli">Christina Juli</name></noRegion><name sortKey="Holzgrabe, Ulrike" sort="Holzgrabe, Ulrike" uniqKey="Holzgrabe U" first="Ulrike" last="Holzgrabe">Ulrike Holzgrabe</name></country><country name="Australie"><noRegion><name sortKey="Sarkar Tyson, Mitali" sort="Sarkar Tyson, Mitali" uniqKey="Sarkar Tyson M" first="Mitali" last="Sarkar-Tyson">Mitali Sarkar-Tyson</name></noRegion></country></tree></affiliations></record>Pour manipuler ce document sous Unix (Dilib)
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