Direct Intracellular Delivery of Benzene Diazonium Ions As Observed by Increased Tyrosine Phosphorylation
A challenge within the field of bioconjugation is developing probes to uncover novel information on proteins and other biomolecules. Intracellular delivery of these probes offers the promise of giving relevant context to this information, and these probes can serve as hypothesis-generating tools wit...
Gespeichert in:
| Veröffentlicht in: | Biochemistry (Easton) 2022-04, Vol.61 (8), p.656-664 |
|---|---|
| Hauptverfasser: | , , , , , |
| Format: | Artikel |
| Sprache: | eng |
| Schlagworte: | |
| Online-Zugang: | Volltext |
| Tags: |
Tag hinzufügen
Keine Tags, Fügen Sie den ersten Tag hinzu!
|
| container_end_page | 664 |
|---|---|
| container_issue | 8 |
| container_start_page | 656 |
| container_title | Biochemistry (Easton) |
| container_volume | 61 |
| creator | Cornejo, Natasha R Amofah, Bismark Lipinski, Austin Langlais, Paul R Ghosh, Indraneel Jewett, John C |
| description | A challenge within the field of bioconjugation is developing probes to uncover novel information on proteins and other biomolecules. Intracellular delivery of these probes offers the promise of giving relevant context to this information, and these probes can serve as hypothesis-generating tools within complex systems. Leveraging the utility of triazabutadiene chemistry, herein, we discuss the development of a probe that undergoes reduction-mediated deprotection to rapidly deliver a benzene diazonium ion (BDI) into cells. The intracellular BDI resulted in an increase in global tyrosine phosphorylation levels. Seeing phosphatase dysregulation as a potential source of this increase, a tyrosine phosphatase (PTP1B) was tested and shown to be both inhibited and covalently modified by the BDI. In addition to the expected azobenzene formation at tyrosine side chains, key reactive histidine residues were also modified. |
| doi_str_mv | 10.1021/acs.biochem.1c00820 |
| format | Article |
| fullrecord | <record><control><sourceid>proquest_pubme</sourceid><recordid>TN_cdi_pubmedcentral_primary_oai_pubmedcentral_nih_gov_9203130</recordid><sourceformat>XML</sourceformat><sourcesystem>PC</sourcesystem><sourcerecordid>2641003784</sourcerecordid><originalsourceid>FETCH-LOGICAL-a445t-cffdde1017a52f09645f4eee0db60be77f8f0d6de543f97c07e08ae6c6eee7fc3</originalsourceid><addsrcrecordid>eNp9kUtr3DAUhUVpaKZpf0GhaNmNJ1cP2-NNIc2k7UAgWaRrIctXHQVbmkr2gPPrq2GmodlkJS76zrmPQ8gnBksGnF1qk5atC2aLw5IZgBWHN2TBSg6FbJryLVkAQFXwpoJz8j6lx1xKqOU7ci5KAVyUfEHc2kU0I934MWqDfT_1OtI19m6PcabB0m_on9AjXTv9FLybBroJPtGrRO_ahHGPHW3nrDcRdcrFwxxDcllwvw1ptw1x7vXogv9AzqzuE348vRfk1_ebh-ufxe3dj8311W2hpSzHwljbdciA1brkFppKllYiInRtBS3WtV1Z6KoOSylsUxuoEVYaK1NlqLZGXJCvR9_d1A7YGTxs1qtddIOOswraqZc_3m3V77BXDQfBBGSDLyeDGP5MmEY1uHQ4jfYYpqR4JRmAqFcyo-KImrxzimif2zBQh5BUDkmdQlKnkLLq8_8TPmv-pZKByyNwUD-GKfp8sFct_wJN_KSO</addsrcrecordid><sourcetype>Open Access Repository</sourcetype><iscdi>true</iscdi><recordtype>article</recordtype><pqid>2641003784</pqid></control><display><type>article</type><title>Direct Intracellular Delivery of Benzene Diazonium Ions As Observed by Increased Tyrosine Phosphorylation</title><source>ACS Publications</source><source>MEDLINE</source><creator>Cornejo, Natasha R ; Amofah, Bismark ; Lipinski, Austin ; Langlais, Paul R ; Ghosh, Indraneel ; Jewett, John C</creator><creatorcontrib>Cornejo, Natasha R ; Amofah, Bismark ; Lipinski, Austin ; Langlais, Paul R ; Ghosh, Indraneel ; Jewett, John C</creatorcontrib><description>A challenge within the field of bioconjugation is developing probes to uncover novel information on proteins and other biomolecules. Intracellular delivery of these probes offers the promise of giving relevant context to this information, and these probes can serve as hypothesis-generating tools within complex systems. Leveraging the utility of triazabutadiene chemistry, herein, we discuss the development of a probe that undergoes reduction-mediated deprotection to rapidly deliver a benzene diazonium ion (BDI) into cells. The intracellular BDI resulted in an increase in global tyrosine phosphorylation levels. Seeing phosphatase dysregulation as a potential source of this increase, a tyrosine phosphatase (PTP1B) was tested and shown to be both inhibited and covalently modified by the BDI. In addition to the expected azobenzene formation at tyrosine side chains, key reactive histidine residues were also modified.</description><identifier>ISSN: 0006-2960</identifier><identifier>EISSN: 1520-4995</identifier><identifier>DOI: 10.1021/acs.biochem.1c00820</identifier><identifier>PMID: 35302352</identifier><language>eng</language><publisher>United States: American Chemical Society</publisher><subject>Benzene ; Ions ; Phosphorylation ; Protein Tyrosine Phosphatase, Non-Receptor Type 1 - metabolism ; Proteins - chemistry ; Tyrosine - metabolism</subject><ispartof>Biochemistry (Easton), 2022-04, Vol.61 (8), p.656-664</ispartof><rights>2022 American Chemical Society</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-a445t-cffdde1017a52f09645f4eee0db60be77f8f0d6de543f97c07e08ae6c6eee7fc3</citedby><cites>FETCH-LOGICAL-a445t-cffdde1017a52f09645f4eee0db60be77f8f0d6de543f97c07e08ae6c6eee7fc3</cites><orcidid>0000-0001-5822-4080</orcidid></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://pubs.acs.org/doi/pdf/10.1021/acs.biochem.1c00820$$EPDF$$P50$$Gacs$$H</linktopdf><linktohtml>$$Uhttps://pubs.acs.org/doi/10.1021/acs.biochem.1c00820$$EHTML$$P50$$Gacs$$H</linktohtml><link.rule.ids>230,314,776,780,881,2752,27053,27901,27902,56713,56763</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/35302352$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Cornejo, Natasha R</creatorcontrib><creatorcontrib>Amofah, Bismark</creatorcontrib><creatorcontrib>Lipinski, Austin</creatorcontrib><creatorcontrib>Langlais, Paul R</creatorcontrib><creatorcontrib>Ghosh, Indraneel</creatorcontrib><creatorcontrib>Jewett, John C</creatorcontrib><title>Direct Intracellular Delivery of Benzene Diazonium Ions As Observed by Increased Tyrosine Phosphorylation</title><title>Biochemistry (Easton)</title><addtitle>Biochemistry</addtitle><description>A challenge within the field of bioconjugation is developing probes to uncover novel information on proteins and other biomolecules. Intracellular delivery of these probes offers the promise of giving relevant context to this information, and these probes can serve as hypothesis-generating tools within complex systems. Leveraging the utility of triazabutadiene chemistry, herein, we discuss the development of a probe that undergoes reduction-mediated deprotection to rapidly deliver a benzene diazonium ion (BDI) into cells. The intracellular BDI resulted in an increase in global tyrosine phosphorylation levels. Seeing phosphatase dysregulation as a potential source of this increase, a tyrosine phosphatase (PTP1B) was tested and shown to be both inhibited and covalently modified by the BDI. In addition to the expected azobenzene formation at tyrosine side chains, key reactive histidine residues were also modified.</description><subject>Benzene</subject><subject>Ions</subject><subject>Phosphorylation</subject><subject>Protein Tyrosine Phosphatase, Non-Receptor Type 1 - metabolism</subject><subject>Proteins - chemistry</subject><subject>Tyrosine - metabolism</subject><issn>0006-2960</issn><issn>1520-4995</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2022</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNp9kUtr3DAUhUVpaKZpf0GhaNmNJ1cP2-NNIc2k7UAgWaRrIctXHQVbmkr2gPPrq2GmodlkJS76zrmPQ8gnBksGnF1qk5atC2aLw5IZgBWHN2TBSg6FbJryLVkAQFXwpoJz8j6lx1xKqOU7ci5KAVyUfEHc2kU0I934MWqDfT_1OtI19m6PcabB0m_on9AjXTv9FLybBroJPtGrRO_ahHGPHW3nrDcRdcrFwxxDcllwvw1ptw1x7vXogv9AzqzuE348vRfk1_ebh-ufxe3dj8311W2hpSzHwljbdciA1brkFppKllYiInRtBS3WtV1Z6KoOSylsUxuoEVYaK1NlqLZGXJCvR9_d1A7YGTxs1qtddIOOswraqZc_3m3V77BXDQfBBGSDLyeDGP5MmEY1uHQ4jfYYpqR4JRmAqFcyo-KImrxzimif2zBQh5BUDkmdQlKnkLLq8_8TPmv-pZKByyNwUD-GKfp8sFct_wJN_KSO</recordid><startdate>20220419</startdate><enddate>20220419</enddate><creator>Cornejo, Natasha R</creator><creator>Amofah, Bismark</creator><creator>Lipinski, Austin</creator><creator>Langlais, Paul R</creator><creator>Ghosh, Indraneel</creator><creator>Jewett, John C</creator><general>American Chemical Society</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><scope>5PM</scope><orcidid>https://orcid.org/0000-0001-5822-4080</orcidid></search><sort><creationdate>20220419</creationdate><title>Direct Intracellular Delivery of Benzene Diazonium Ions As Observed by Increased Tyrosine Phosphorylation</title><author>Cornejo, Natasha R ; Amofah, Bismark ; Lipinski, Austin ; Langlais, Paul R ; Ghosh, Indraneel ; Jewett, John C</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-a445t-cffdde1017a52f09645f4eee0db60be77f8f0d6de543f97c07e08ae6c6eee7fc3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2022</creationdate><topic>Benzene</topic><topic>Ions</topic><topic>Phosphorylation</topic><topic>Protein Tyrosine Phosphatase, Non-Receptor Type 1 - metabolism</topic><topic>Proteins - chemistry</topic><topic>Tyrosine - metabolism</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Cornejo, Natasha R</creatorcontrib><creatorcontrib>Amofah, Bismark</creatorcontrib><creatorcontrib>Lipinski, Austin</creatorcontrib><creatorcontrib>Langlais, Paul R</creatorcontrib><creatorcontrib>Ghosh, Indraneel</creatorcontrib><creatorcontrib>Jewett, John C</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><collection>PubMed Central (Full Participant titles)</collection><jtitle>Biochemistry (Easton)</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Cornejo, Natasha R</au><au>Amofah, Bismark</au><au>Lipinski, Austin</au><au>Langlais, Paul R</au><au>Ghosh, Indraneel</au><au>Jewett, John C</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Direct Intracellular Delivery of Benzene Diazonium Ions As Observed by Increased Tyrosine Phosphorylation</atitle><jtitle>Biochemistry (Easton)</jtitle><addtitle>Biochemistry</addtitle><date>2022-04-19</date><risdate>2022</risdate><volume>61</volume><issue>8</issue><spage>656</spage><epage>664</epage><pages>656-664</pages><issn>0006-2960</issn><eissn>1520-4995</eissn><abstract>A challenge within the field of bioconjugation is developing probes to uncover novel information on proteins and other biomolecules. Intracellular delivery of these probes offers the promise of giving relevant context to this information, and these probes can serve as hypothesis-generating tools within complex systems. Leveraging the utility of triazabutadiene chemistry, herein, we discuss the development of a probe that undergoes reduction-mediated deprotection to rapidly deliver a benzene diazonium ion (BDI) into cells. The intracellular BDI resulted in an increase in global tyrosine phosphorylation levels. Seeing phosphatase dysregulation as a potential source of this increase, a tyrosine phosphatase (PTP1B) was tested and shown to be both inhibited and covalently modified by the BDI. In addition to the expected azobenzene formation at tyrosine side chains, key reactive histidine residues were also modified.</abstract><cop>United States</cop><pub>American Chemical Society</pub><pmid>35302352</pmid><doi>10.1021/acs.biochem.1c00820</doi><tpages>9</tpages><orcidid>https://orcid.org/0000-0001-5822-4080</orcidid><oa>free_for_read</oa></addata></record> |
| fulltext | fulltext |
| identifier | ISSN: 0006-2960 |
| ispartof | Biochemistry (Easton), 2022-04, Vol.61 (8), p.656-664 |
| issn | 0006-2960 1520-4995 |
| language | eng |
| recordid | cdi_pubmedcentral_primary_oai_pubmedcentral_nih_gov_9203130 |
| source | ACS Publications; MEDLINE |
| subjects | Benzene Ions Phosphorylation Protein Tyrosine Phosphatase, Non-Receptor Type 1 - metabolism Proteins - chemistry Tyrosine - metabolism |
| title | Direct Intracellular Delivery of Benzene Diazonium Ions As Observed by Increased Tyrosine Phosphorylation |
| url | https://sfx.bib-bvb.de/sfx_tum?ctx_ver=Z39.88-2004&ctx_enc=info:ofi/enc:UTF-8&ctx_tim=2025-02-02T16%3A42%3A07IST&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=Direct%20Intracellular%20Delivery%20of%20Benzene%20Diazonium%20Ions%20As%20Observed%20by%20Increased%20Tyrosine%20Phosphorylation&rft.jtitle=Biochemistry%20(Easton)&rft.au=Cornejo,%20Natasha%20R&rft.date=2022-04-19&rft.volume=61&rft.issue=8&rft.spage=656&rft.epage=664&rft.pages=656-664&rft.issn=0006-2960&rft.eissn=1520-4995&rft_id=info:doi/10.1021/acs.biochem.1c00820&rft_dat=%3Cproquest_pubme%3E2641003784%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=2641003784&rft_id=info:pmid/35302352&rfr_iscdi=true |