Development of a quantitative fluorescence-based ligand-binding assay
A major goal of biology is to develop a quantitative ligand-binding assay that does not involve the use of radioactivity. Existing fluorescence-based assays have a serious drawback due to fluorescence quenching that accompanies the binding of fluorescently-labeled ligands to their receptors. This li...
Gespeichert in:
Veröffentlicht in: | Scientific reports 2016-05, Vol.6 (1), p.25769-25769, Article 25769 |
---|---|
Hauptverfasser: | , , |
Format: | Artikel |
Sprache: | eng |
Schlagworte: | |
Online-Zugang: | Volltext |
Tags: |
Tag hinzufügen
Keine Tags, Fügen Sie den ersten Tag hinzu!
|
container_end_page | 25769 |
---|---|
container_issue | 1 |
container_start_page | 25769 |
container_title | Scientific reports |
container_volume | 6 |
creator | Breen, Conor J. Raverdeau, Mathilde Voorheis, H. Paul |
description | A major goal of biology is to develop a quantitative ligand-binding assay that does not involve the use of radioactivity. Existing fluorescence-based assays have a serious drawback due to fluorescence quenching that accompanies the binding of fluorescently-labeled ligands to their receptors. This limitation of existing fluorescence-based assays prevents the number of cellular receptors under investigation from being accurately measured. We have developed a method where FITC-labeled proteins bound to a cell surface are proteolyzed extensively to eliminate fluorescence quenching and then the fluorescence of the resulting sample is compared to that of a known concentration of the proteolyzed FITC-protein employed. This step enables the number of cellular receptors to be measured quantitatively. We expect that this method will provide researchers with a viable alternative to the use of radioactivity in ligand binding assays. |
doi_str_mv | 10.1038/srep25769 |
format | Article |
fullrecord | <record><control><sourceid>proquest_pubme</sourceid><recordid>TN_cdi_pubmedcentral_primary_oai_pubmedcentral_nih_gov_4861924</recordid><sourceformat>XML</sourceformat><sourcesystem>PC</sourcesystem><sourcerecordid>1788227379</sourcerecordid><originalsourceid>FETCH-LOGICAL-c504t-30e96498381b4ab9f6c2d4b7716d58961353ad489f39bd4fec933c200b02e4ee3</originalsourceid><addsrcrecordid>eNplkU1LAzEQhoMoVqoH_4AseFFhNV-bTS6CaP0AwYueQ3Z3tqZsk5rsFvrvjVRL1bnMwDy88w4vQscEXxLM5FUMsKBFKdQOOqCYFzlllO5uzSN0FOMMpyqo4kTtoxEtiSBU4QM0uYMldH4xB9dnvs1M9jEY19ve9HYJWdsNPkCswdWQVyZCk3V2alyTV9Y11k0zE6NZHaK91nQRjr77GL3dT15vH_Pnl4en25vnvC4w73OGQQmuJJOk4qZSrahpw6syuWkKqQRhBTMNl6plqmp4C7VirKYYV5gCB2BjdL3WXQzVHJpkqw-m04tg5yastDdW_944-66nfqm5FERRngTOvgWC_xgg9npu03ddZxz4IWpSSklpyUqV0NM_6MwPwaX3NJFKCsEFEYk6X1N18DFF0W7MEKy_8tGbfBJ7su1-Q_6kkYCLNRDTyk0hbJ38p_YJ6JOZ1w</addsrcrecordid><sourcetype>Open Access Repository</sourcetype><iscdi>true</iscdi><recordtype>article</recordtype><pqid>1898664616</pqid></control><display><type>article</type><title>Development of a quantitative fluorescence-based ligand-binding assay</title><source>DOAJ Directory of Open Access Journals</source><source>Nature Free</source><source>EZB-FREE-00999 freely available EZB journals</source><source>PubMed Central</source><source>Springer Nature OA/Free Journals</source><source>Free Full-Text Journals in Chemistry</source><creator>Breen, Conor J. ; Raverdeau, Mathilde ; Voorheis, H. Paul</creator><creatorcontrib>Breen, Conor J. ; Raverdeau, Mathilde ; Voorheis, H. Paul</creatorcontrib><description>A major goal of biology is to develop a quantitative ligand-binding assay that does not involve the use of radioactivity. Existing fluorescence-based assays have a serious drawback due to fluorescence quenching that accompanies the binding of fluorescently-labeled ligands to their receptors. This limitation of existing fluorescence-based assays prevents the number of cellular receptors under investigation from being accurately measured. We have developed a method where FITC-labeled proteins bound to a cell surface are proteolyzed extensively to eliminate fluorescence quenching and then the fluorescence of the resulting sample is compared to that of a known concentration of the proteolyzed FITC-protein employed. This step enables the number of cellular receptors to be measured quantitatively. We expect that this method will provide researchers with a viable alternative to the use of radioactivity in ligand binding assays.</description><identifier>ISSN: 2045-2322</identifier><identifier>EISSN: 2045-2322</identifier><identifier>DOI: 10.1038/srep25769</identifier><identifier>PMID: 27161290</identifier><language>eng</language><publisher>London: Nature Publishing Group UK</publisher><subject>14/10 ; 631/1647/2196/2197 ; 631/45/468 ; Cell surface ; Fluorescence ; Humanities and Social Sciences ; Ligands ; multidisciplinary ; Radioactivity ; Science</subject><ispartof>Scientific reports, 2016-05, Vol.6 (1), p.25769-25769, Article 25769</ispartof><rights>The Author(s) 2016</rights><rights>Copyright Nature Publishing Group May 2016</rights><rights>Copyright © 2016, Macmillan Publishers Limited 2016 Macmillan Publishers Limited</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c504t-30e96498381b4ab9f6c2d4b7716d58961353ad489f39bd4fec933c200b02e4ee3</citedby><cites>FETCH-LOGICAL-c504t-30e96498381b4ab9f6c2d4b7716d58961353ad489f39bd4fec933c200b02e4ee3</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://www.ncbi.nlm.nih.gov/pmc/articles/PMC4861924/pdf/$$EPDF$$P50$$Gpubmedcentral$$Hfree_for_read</linktopdf><linktohtml>$$Uhttps://www.ncbi.nlm.nih.gov/pmc/articles/PMC4861924/$$EHTML$$P50$$Gpubmedcentral$$Hfree_for_read</linktohtml><link.rule.ids>230,315,728,781,785,865,886,27929,27930,41125,42194,51581,53796,53798</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/27161290$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Breen, Conor J.</creatorcontrib><creatorcontrib>Raverdeau, Mathilde</creatorcontrib><creatorcontrib>Voorheis, H. Paul</creatorcontrib><title>Development of a quantitative fluorescence-based ligand-binding assay</title><title>Scientific reports</title><addtitle>Sci Rep</addtitle><addtitle>Sci Rep</addtitle><description>A major goal of biology is to develop a quantitative ligand-binding assay that does not involve the use of radioactivity. Existing fluorescence-based assays have a serious drawback due to fluorescence quenching that accompanies the binding of fluorescently-labeled ligands to their receptors. This limitation of existing fluorescence-based assays prevents the number of cellular receptors under investigation from being accurately measured. We have developed a method where FITC-labeled proteins bound to a cell surface are proteolyzed extensively to eliminate fluorescence quenching and then the fluorescence of the resulting sample is compared to that of a known concentration of the proteolyzed FITC-protein employed. This step enables the number of cellular receptors to be measured quantitatively. We expect that this method will provide researchers with a viable alternative to the use of radioactivity in ligand binding assays.</description><subject>14/10</subject><subject>631/1647/2196/2197</subject><subject>631/45/468</subject><subject>Cell surface</subject><subject>Fluorescence</subject><subject>Humanities and Social Sciences</subject><subject>Ligands</subject><subject>multidisciplinary</subject><subject>Radioactivity</subject><subject>Science</subject><issn>2045-2322</issn><issn>2045-2322</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2016</creationdate><recordtype>article</recordtype><sourceid>C6C</sourceid><sourceid>ABUWG</sourceid><sourceid>AFKRA</sourceid><sourceid>AZQEC</sourceid><sourceid>BENPR</sourceid><sourceid>CCPQU</sourceid><sourceid>DWQXO</sourceid><sourceid>GNUQQ</sourceid><recordid>eNplkU1LAzEQhoMoVqoH_4AseFFhNV-bTS6CaP0AwYueQ3Z3tqZsk5rsFvrvjVRL1bnMwDy88w4vQscEXxLM5FUMsKBFKdQOOqCYFzlllO5uzSN0FOMMpyqo4kTtoxEtiSBU4QM0uYMldH4xB9dnvs1M9jEY19ve9HYJWdsNPkCswdWQVyZCk3V2alyTV9Y11k0zE6NZHaK91nQRjr77GL3dT15vH_Pnl4en25vnvC4w73OGQQmuJJOk4qZSrahpw6syuWkKqQRhBTMNl6plqmp4C7VirKYYV5gCB2BjdL3WXQzVHJpkqw-m04tg5yastDdW_944-66nfqm5FERRngTOvgWC_xgg9npu03ddZxz4IWpSSklpyUqV0NM_6MwPwaX3NJFKCsEFEYk6X1N18DFF0W7MEKy_8tGbfBJ7su1-Q_6kkYCLNRDTyk0hbJ38p_YJ6JOZ1w</recordid><startdate>20160510</startdate><enddate>20160510</enddate><creator>Breen, Conor J.</creator><creator>Raverdeau, Mathilde</creator><creator>Voorheis, H. Paul</creator><general>Nature Publishing Group UK</general><general>Nature Publishing Group</general><scope>C6C</scope><scope>NPM</scope><scope>AAYXX</scope><scope>CITATION</scope><scope>3V.</scope><scope>7X7</scope><scope>7XB</scope><scope>88A</scope><scope>88E</scope><scope>88I</scope><scope>8FE</scope><scope>8FH</scope><scope>8FI</scope><scope>8FJ</scope><scope>8FK</scope><scope>ABUWG</scope><scope>AFKRA</scope><scope>AZQEC</scope><scope>BBNVY</scope><scope>BENPR</scope><scope>BHPHI</scope><scope>CCPQU</scope><scope>DWQXO</scope><scope>FYUFA</scope><scope>GHDGH</scope><scope>GNUQQ</scope><scope>HCIFZ</scope><scope>K9.</scope><scope>LK8</scope><scope>M0S</scope><scope>M1P</scope><scope>M2P</scope><scope>M7P</scope><scope>PIMPY</scope><scope>PQEST</scope><scope>PQQKQ</scope><scope>PQUKI</scope><scope>Q9U</scope><scope>7X8</scope><scope>5PM</scope></search><sort><creationdate>20160510</creationdate><title>Development of a quantitative fluorescence-based ligand-binding assay</title><author>Breen, Conor J. ; Raverdeau, Mathilde ; Voorheis, H. Paul</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c504t-30e96498381b4ab9f6c2d4b7716d58961353ad489f39bd4fec933c200b02e4ee3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2016</creationdate><topic>14/10</topic><topic>631/1647/2196/2197</topic><topic>631/45/468</topic><topic>Cell surface</topic><topic>Fluorescence</topic><topic>Humanities and Social Sciences</topic><topic>Ligands</topic><topic>multidisciplinary</topic><topic>Radioactivity</topic><topic>Science</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Breen, Conor J.</creatorcontrib><creatorcontrib>Raverdeau, Mathilde</creatorcontrib><creatorcontrib>Voorheis, H. Paul</creatorcontrib><collection>Springer Nature OA/Free Journals</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>ProQuest Central (Corporate)</collection><collection>Health & Medical Collection</collection><collection>ProQuest Central (purchase pre-March 2016)</collection><collection>Biology Database (Alumni Edition)</collection><collection>Medical Database (Alumni Edition)</collection><collection>Science Database (Alumni Edition)</collection><collection>ProQuest SciTech Collection</collection><collection>ProQuest Natural Science Collection</collection><collection>Hospital Premium Collection</collection><collection>Hospital Premium Collection (Alumni Edition)</collection><collection>ProQuest Central (Alumni) (purchase pre-March 2016)</collection><collection>ProQuest Central (Alumni Edition)</collection><collection>ProQuest Central UK/Ireland</collection><collection>ProQuest Central Essentials</collection><collection>Biological Science Collection</collection><collection>ProQuest Central</collection><collection>Natural Science Collection</collection><collection>ProQuest One Community College</collection><collection>ProQuest Central Korea</collection><collection>Health Research Premium Collection</collection><collection>Health Research Premium Collection (Alumni)</collection><collection>ProQuest Central Student</collection><collection>SciTech Premium Collection</collection><collection>ProQuest Health & Medical Complete (Alumni)</collection><collection>ProQuest Biological Science Collection</collection><collection>Health & Medical Collection (Alumni Edition)</collection><collection>Medical Database</collection><collection>Science Database</collection><collection>Biological Science Database</collection><collection>Access via ProQuest (Open Access)</collection><collection>ProQuest One Academic Eastern Edition (DO NOT USE)</collection><collection>ProQuest One Academic</collection><collection>ProQuest One Academic UKI Edition</collection><collection>ProQuest Central Basic</collection><collection>MEDLINE - Academic</collection><collection>PubMed Central (Full Participant titles)</collection><jtitle>Scientific reports</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Breen, Conor J.</au><au>Raverdeau, Mathilde</au><au>Voorheis, H. Paul</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Development of a quantitative fluorescence-based ligand-binding assay</atitle><jtitle>Scientific reports</jtitle><stitle>Sci Rep</stitle><addtitle>Sci Rep</addtitle><date>2016-05-10</date><risdate>2016</risdate><volume>6</volume><issue>1</issue><spage>25769</spage><epage>25769</epage><pages>25769-25769</pages><artnum>25769</artnum><issn>2045-2322</issn><eissn>2045-2322</eissn><abstract>A major goal of biology is to develop a quantitative ligand-binding assay that does not involve the use of radioactivity. Existing fluorescence-based assays have a serious drawback due to fluorescence quenching that accompanies the binding of fluorescently-labeled ligands to their receptors. This limitation of existing fluorescence-based assays prevents the number of cellular receptors under investigation from being accurately measured. We have developed a method where FITC-labeled proteins bound to a cell surface are proteolyzed extensively to eliminate fluorescence quenching and then the fluorescence of the resulting sample is compared to that of a known concentration of the proteolyzed FITC-protein employed. This step enables the number of cellular receptors to be measured quantitatively. We expect that this method will provide researchers with a viable alternative to the use of radioactivity in ligand binding assays.</abstract><cop>London</cop><pub>Nature Publishing Group UK</pub><pmid>27161290</pmid><doi>10.1038/srep25769</doi><tpages>1</tpages><oa>free_for_read</oa></addata></record> |
fulltext | fulltext |
identifier | ISSN: 2045-2322 |
ispartof | Scientific reports, 2016-05, Vol.6 (1), p.25769-25769, Article 25769 |
issn | 2045-2322 2045-2322 |
language | eng |
recordid | cdi_pubmedcentral_primary_oai_pubmedcentral_nih_gov_4861924 |
source | DOAJ Directory of Open Access Journals; Nature Free; EZB-FREE-00999 freely available EZB journals; PubMed Central; Springer Nature OA/Free Journals; Free Full-Text Journals in Chemistry |
subjects | 14/10 631/1647/2196/2197 631/45/468 Cell surface Fluorescence Humanities and Social Sciences Ligands multidisciplinary Radioactivity Science |
title | Development of a quantitative fluorescence-based ligand-binding assay |
url | https://sfx.bib-bvb.de/sfx_tum?ctx_ver=Z39.88-2004&ctx_enc=info:ofi/enc:UTF-8&ctx_tim=2024-12-15T01%3A56%3A51IST&url_ver=Z39.88-2004&url_ctx_fmt=infofi/fmt:kev:mtx:ctx&rfr_id=info:sid/primo.exlibrisgroup.com:primo3-Article-proquest_pubme&rft_val_fmt=info:ofi/fmt:kev:mtx:journal&rft.genre=article&rft.atitle=Development%20of%20a%20quantitative%20fluorescence-based%20ligand-binding%20assay&rft.jtitle=Scientific%20reports&rft.au=Breen,%20Conor%20J.&rft.date=2016-05-10&rft.volume=6&rft.issue=1&rft.spage=25769&rft.epage=25769&rft.pages=25769-25769&rft.artnum=25769&rft.issn=2045-2322&rft.eissn=2045-2322&rft_id=info:doi/10.1038/srep25769&rft_dat=%3Cproquest_pubme%3E1788227379%3C/proquest_pubme%3E%3Curl%3E%3C/url%3E&disable_directlink=true&sfx.directlink=off&sfx.report_link=0&rft_id=info:oai/&rft_pqid=1898664616&rft_id=info:pmid/27161290&rfr_iscdi=true |