Protein labeling and crosslinking by covalent aptamers

In this chapter, a new approach to the selective modification of native proteins is discussed, using electrophilic covalent aptamers. These biochemical tools are generated through the site-specific incorporation of a label-transferring or crosslinking electrophile into a DNA aptamer. Covalent aptame...

Ausführliche Beschreibung

Gespeichert in:
Bibliographische Detailangaben
Veröffentlicht in:Methods in enzymology 2023-01, Vol.682, p.413-428
Hauptverfasser: Cacace, Mary, Tivon, Yaniv, Deiters, Alexander
Format: Artikel
Sprache:eng
Schlagworte:
Online-Zugang:Volltext
Tags: Tag hinzufügen
Keine Tags, Fügen Sie den ersten Tag hinzu!
container_end_page 428
container_issue
container_start_page 413
container_title Methods in enzymology
container_volume 682
creator Cacace, Mary
Tivon, Yaniv
Deiters, Alexander
description In this chapter, a new approach to the selective modification of native proteins is discussed, using electrophilic covalent aptamers. These biochemical tools are generated through the site-specific incorporation of a label-transferring or crosslinking electrophile into a DNA aptamer. Covalent aptamers provide the ability to transfer a variety of functional handles to a protein of interest or to irreversibly crosslink to the target. Methods for the aptamer-mediated labeling and crosslinking of thrombin are described. Thrombin labeling is fast and selective, in both simple buffer and in human plasma and outcompetes nuclease-mediated degradation. This approach provides facile, sensitive detection of labeled protein by western blot, SDS-PAGE, and mass spectrometry.
doi_str_mv 10.1016/bs.mie.2022.08.053
format Article
fullrecord <record><control><sourceid>proquest_pubme</sourceid><recordid>TN_cdi_pubmedcentral_primary_oai_pubmedcentral_nih_gov_10725707</recordid><sourceformat>XML</sourceformat><sourcesystem>PC</sourcesystem><sourcerecordid>2790052471</sourcerecordid><originalsourceid>FETCH-LOGICAL-p267t-acc58cdca5543a7a578b8a2a9f61c1fdf726aa8a78eadcd4b1cf8e8e5c0bf673</originalsourceid><addsrcrecordid>eNpVkEtPwzAQhC0EoqXwBzigHLkkrJ3Y65wQqnhJleDQu7V2nBLIizit1H9PKwqC02h3Vt-shrFLDgkHrm5sSJrKJwKESEAnINMjNuVSYoy51sdsCoAqVhrzCTsL4R1AoM75KZukKs80Qj5l6nXoRl-1UU3W11W7iqgtIjd0Ieymj_3CbiPXbaj27RhRP1Ljh3DOTkqqg7846IwtH-6X86d48fL4PL9bxL1QOMbknNSucCRllhKSRG01CcpLxR0vixKFItKE2lPhisxyV2qvvXRgS4XpjN1-Y_u1bXzhdi8MVJt-qBoatqajyvx32urNrLqN4YBCIuwJ1wfC0H2ufRhNUwXn65pa362DEZgDSJEh351e_Q37TfkpK_0CVTRv2Q</addsrcrecordid><sourcetype>Open Access Repository</sourcetype><iscdi>true</iscdi><recordtype>article</recordtype><pqid>2790052471</pqid></control><display><type>article</type><title>Protein labeling and crosslinking by covalent aptamers</title><source>MEDLINE</source><source>Access via ScienceDirect (Elsevier)</source><creator>Cacace, Mary ; Tivon, Yaniv ; Deiters, Alexander</creator><creatorcontrib>Cacace, Mary ; Tivon, Yaniv ; Deiters, Alexander</creatorcontrib><description>In this chapter, a new approach to the selective modification of native proteins is discussed, using electrophilic covalent aptamers. These biochemical tools are generated through the site-specific incorporation of a label-transferring or crosslinking electrophile into a DNA aptamer. Covalent aptamers provide the ability to transfer a variety of functional handles to a protein of interest or to irreversibly crosslink to the target. Methods for the aptamer-mediated labeling and crosslinking of thrombin are described. Thrombin labeling is fast and selective, in both simple buffer and in human plasma and outcompetes nuclease-mediated degradation. This approach provides facile, sensitive detection of labeled protein by western blot, SDS-PAGE, and mass spectrometry.</description><identifier>ISSN: 0076-6879</identifier><identifier>EISSN: 1557-7988</identifier><identifier>DOI: 10.1016/bs.mie.2022.08.053</identifier><identifier>PMID: 36948709</identifier><language>eng</language><publisher>United States</publisher><subject>Aptamers, Nucleotide - chemistry ; Humans ; Mass Spectrometry ; Proteins ; Thrombin - analysis</subject><ispartof>Methods in enzymology, 2023-01, Vol.682, p.413-428</ispartof><rights>Copyright © 2023 Elsevier Inc. All rights reserved.</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><link.rule.ids>230,315,781,785,886,27928,27929</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/36948709$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Cacace, Mary</creatorcontrib><creatorcontrib>Tivon, Yaniv</creatorcontrib><creatorcontrib>Deiters, Alexander</creatorcontrib><title>Protein labeling and crosslinking by covalent aptamers</title><title>Methods in enzymology</title><addtitle>Methods Enzymol</addtitle><description>In this chapter, a new approach to the selective modification of native proteins is discussed, using electrophilic covalent aptamers. These biochemical tools are generated through the site-specific incorporation of a label-transferring or crosslinking electrophile into a DNA aptamer. Covalent aptamers provide the ability to transfer a variety of functional handles to a protein of interest or to irreversibly crosslink to the target. Methods for the aptamer-mediated labeling and crosslinking of thrombin are described. Thrombin labeling is fast and selective, in both simple buffer and in human plasma and outcompetes nuclease-mediated degradation. This approach provides facile, sensitive detection of labeled protein by western blot, SDS-PAGE, and mass spectrometry.</description><subject>Aptamers, Nucleotide - chemistry</subject><subject>Humans</subject><subject>Mass Spectrometry</subject><subject>Proteins</subject><subject>Thrombin - analysis</subject><issn>0076-6879</issn><issn>1557-7988</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2023</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNpVkEtPwzAQhC0EoqXwBzigHLkkrJ3Y65wQqnhJleDQu7V2nBLIizit1H9PKwqC02h3Vt-shrFLDgkHrm5sSJrKJwKESEAnINMjNuVSYoy51sdsCoAqVhrzCTsL4R1AoM75KZukKs80Qj5l6nXoRl-1UU3W11W7iqgtIjd0Ieymj_3CbiPXbaj27RhRP1Ljh3DOTkqqg7846IwtH-6X86d48fL4PL9bxL1QOMbknNSucCRllhKSRG01CcpLxR0vixKFItKE2lPhisxyV2qvvXRgS4XpjN1-Y_u1bXzhdi8MVJt-qBoatqajyvx32urNrLqN4YBCIuwJ1wfC0H2ufRhNUwXn65pa362DEZgDSJEh351e_Q37TfkpK_0CVTRv2Q</recordid><startdate>20230101</startdate><enddate>20230101</enddate><creator>Cacace, Mary</creator><creator>Tivon, Yaniv</creator><creator>Deiters, Alexander</creator><scope>CGR</scope><scope>CUY</scope><scope>CVF</scope><scope>ECM</scope><scope>EIF</scope><scope>NPM</scope><scope>7X8</scope><scope>5PM</scope></search><sort><creationdate>20230101</creationdate><title>Protein labeling and crosslinking by covalent aptamers</title><author>Cacace, Mary ; Tivon, Yaniv ; Deiters, Alexander</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-p267t-acc58cdca5543a7a578b8a2a9f61c1fdf726aa8a78eadcd4b1cf8e8e5c0bf673</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2023</creationdate><topic>Aptamers, Nucleotide - chemistry</topic><topic>Humans</topic><topic>Mass Spectrometry</topic><topic>Proteins</topic><topic>Thrombin - analysis</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Cacace, Mary</creatorcontrib><creatorcontrib>Tivon, Yaniv</creatorcontrib><creatorcontrib>Deiters, Alexander</creatorcontrib><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>MEDLINE - Academic</collection><collection>PubMed Central (Full Participant titles)</collection><jtitle>Methods in enzymology</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Cacace, Mary</au><au>Tivon, Yaniv</au><au>Deiters, Alexander</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Protein labeling and crosslinking by covalent aptamers</atitle><jtitle>Methods in enzymology</jtitle><addtitle>Methods Enzymol</addtitle><date>2023-01-01</date><risdate>2023</risdate><volume>682</volume><spage>413</spage><epage>428</epage><pages>413-428</pages><issn>0076-6879</issn><eissn>1557-7988</eissn><abstract>In this chapter, a new approach to the selective modification of native proteins is discussed, using electrophilic covalent aptamers. These biochemical tools are generated through the site-specific incorporation of a label-transferring or crosslinking electrophile into a DNA aptamer. Covalent aptamers provide the ability to transfer a variety of functional handles to a protein of interest or to irreversibly crosslink to the target. Methods for the aptamer-mediated labeling and crosslinking of thrombin are described. Thrombin labeling is fast and selective, in both simple buffer and in human plasma and outcompetes nuclease-mediated degradation. This approach provides facile, sensitive detection of labeled protein by western blot, SDS-PAGE, and mass spectrometry.</abstract><cop>United States</cop><pmid>36948709</pmid><doi>10.1016/bs.mie.2022.08.053</doi><tpages>16</tpages></addata></record>
fulltext fulltext
identifier ISSN: 0076-6879
ispartof Methods in enzymology, 2023-01, Vol.682, p.413-428
issn 0076-6879
1557-7988
language eng
recordid cdi_pubmedcentral_primary_oai_pubmedcentral_nih_gov_10725707
source MEDLINE; Access via ScienceDirect (Elsevier)
subjects Aptamers, Nucleotide - chemistry
Humans
Mass Spectrometry
Proteins
Thrombin - analysis
title Protein labeling and crosslinking by covalent aptamers
url https://sfx.bib-bvb.de/sfx_tum?ctx_ver=Z39.88-2004&ctx_enc=info:ofi/enc:UTF-8&ctx_tim=2024-12-17T09%3A21%3A08IST&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=Protein%20labeling%20and%20crosslinking%20by%20covalent%20aptamers&rft.jtitle=Methods%20in%20enzymology&rft.au=Cacace,%20Mary&rft.date=2023-01-01&rft.volume=682&rft.spage=413&rft.epage=428&rft.pages=413-428&rft.issn=0076-6879&rft.eissn=1557-7988&rft_id=info:doi/10.1016/bs.mie.2022.08.053&rft_dat=%3Cproquest_pubme%3E2790052471%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=2790052471&rft_id=info:pmid/36948709&rfr_iscdi=true