Live‐Cell Protein Sulfonylation Based on Proximity‐driven N‐Sulfonyl Pyridone Chemistry
The development of bioorthogonal approaches for labeling of endogenous proteins under the multimolecular crowding conditions of live cells is highly desirable for the analysis and engineering of proteins without using genetic manipulation. N‐Sulfonyl pyridone (SP) is reported as a new reactive group...
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| Veröffentlicht in: | Angewandte Chemie International Edition 2018-01, Vol.57 (3), p.659-662 |
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| container_title | Angewandte Chemie International Edition |
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| creator | Matsuo, Kazuya Nishikawa, Yuki Masuda, Marie Hamachi, Itaru |
| description | The development of bioorthogonal approaches for labeling of endogenous proteins under the multimolecular crowding conditions of live cells is highly desirable for the analysis and engineering of proteins without using genetic manipulation. N‐Sulfonyl pyridone (SP) is reported as a new reactive group for protein sulfonylation. The ligand‐directed SP chemistry was able to modify not only purified proteins in vitro, but also endogenous ones on the surface of and inside live cells selectively and rapidly, which allowed to convert endogenous proteins to FRET‐based biosensors in situ.
Ligand‐directed N‐sulfonyl pyridone chemistry afforded the specific sulfonylation of endogenous proteins without disturbing their original nature. This chemical strategy allowed the simple conversion of endogenous proteins in live cell habitats into semisynthetic FRET biosensors for the analysis of the dynamic process in protein–ligand (small molecule) interactions. |
| doi_str_mv | 10.1002/anie.201707972 |
| format | Article |
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Ligand‐directed N‐sulfonyl pyridone chemistry afforded the specific sulfonylation of endogenous proteins without disturbing their original nature. This chemical strategy allowed the simple conversion of endogenous proteins in live cell habitats into semisynthetic FRET biosensors for the analysis of the dynamic process in protein–ligand (small molecule) interactions.</description><edition>International ed. in English</edition><identifier>ISSN: 1433-7851</identifier><identifier>EISSN: 1521-3773</identifier><identifier>DOI: 10.1002/anie.201707972</identifier><identifier>PMID: 29193552</identifier><language>eng</language><publisher>Germany: Wiley Subscription Services, Inc</publisher><subject>Biosensors ; Fluorescence resonance energy transfer ; FRET biosensors ; intracellular protein labeling ; N-sulfonyl pyridones ; Proteins ; traceless affinity sulfonylation</subject><ispartof>Angewandte Chemie International Edition, 2018-01, Vol.57 (3), p.659-662</ispartof><rights>2018 Wiley‐VCH Verlag GmbH & Co. KGaA, Weinheim</rights><rights>2018 Wiley-VCH Verlag GmbH & Co. KGaA, Weinheim.</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c4762-b6f2bb3e20a8a25f6e790c35579c3f53c1dfce05abf911e3ccada0a73fbd14d73</citedby><cites>FETCH-LOGICAL-c4762-b6f2bb3e20a8a25f6e790c35579c3f53c1dfce05abf911e3ccada0a73fbd14d73</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://onlinelibrary.wiley.com/doi/pdf/10.1002%2Fanie.201707972$$EPDF$$P50$$Gwiley$$H</linktopdf><linktohtml>$$Uhttps://onlinelibrary.wiley.com/doi/full/10.1002%2Fanie.201707972$$EHTML$$P50$$Gwiley$$H</linktohtml><link.rule.ids>314,776,780,1411,27901,27902,45550,45551</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/29193552$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Matsuo, Kazuya</creatorcontrib><creatorcontrib>Nishikawa, Yuki</creatorcontrib><creatorcontrib>Masuda, Marie</creatorcontrib><creatorcontrib>Hamachi, Itaru</creatorcontrib><title>Live‐Cell Protein Sulfonylation Based on Proximity‐driven N‐Sulfonyl Pyridone Chemistry</title><title>Angewandte Chemie International Edition</title><addtitle>Angew Chem Int Ed Engl</addtitle><description>The development of bioorthogonal approaches for labeling of endogenous proteins under the multimolecular crowding conditions of live cells is highly desirable for the analysis and engineering of proteins without using genetic manipulation. N‐Sulfonyl pyridone (SP) is reported as a new reactive group for protein sulfonylation. The ligand‐directed SP chemistry was able to modify not only purified proteins in vitro, but also endogenous ones on the surface of and inside live cells selectively and rapidly, which allowed to convert endogenous proteins to FRET‐based biosensors in situ.
Ligand‐directed N‐sulfonyl pyridone chemistry afforded the specific sulfonylation of endogenous proteins without disturbing their original nature. This chemical strategy allowed the simple conversion of endogenous proteins in live cell habitats into semisynthetic FRET biosensors for the analysis of the dynamic process in protein–ligand (small molecule) interactions.</description><subject>Biosensors</subject><subject>Fluorescence resonance energy transfer</subject><subject>FRET biosensors</subject><subject>intracellular protein labeling</subject><subject>N-sulfonyl pyridones</subject><subject>Proteins</subject><subject>traceless affinity sulfonylation</subject><issn>1433-7851</issn><issn>1521-3773</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2018</creationdate><recordtype>article</recordtype><recordid>eNqFkMtOwzAQRS0EolDYskSR2LBJ8SOJ42WpykOqChKwRJbjjIVRmhQ7AbLjE_hGvgSjUpDYsJorzZk7MxehA4JHBGN6omoLI4oJx1xwuoF2SEpJzDhnm0EnjMU8T8kA7Xr_GPg8x9k2GlBBBEtTuoPuZ_YZPt7eJ1BV0bVrWrB1dNNVpqn7SrW2qaNT5aGMggjtV7uwbR_40oW5OpoHuaaj697ZsqkhmjzAwvrW9Xtoy6jKw_53HaK7s-nt5CKeXZ1fTsazWCc8o3GRGVoUDChWuaKpyYALrMOBXGhmUqZJaTTgVBVGEAJMa1UqrDgzRUmSkrMhOl75Ll3z1IFvZdivw0uqhqbzkghOsiTBmAX06A_62HSuDtdJinGWk0TkeaBGK0q7xnsHRi6dXSjXS4LlV_DyK3j5E3wYOPy27YoFlD_4OukAiBXwYivo_7GT4_nl9Nf8ExZ1k44</recordid><startdate>20180115</startdate><enddate>20180115</enddate><creator>Matsuo, Kazuya</creator><creator>Nishikawa, Yuki</creator><creator>Masuda, Marie</creator><creator>Hamachi, Itaru</creator><general>Wiley Subscription Services, Inc</general><scope>NPM</scope><scope>AAYXX</scope><scope>CITATION</scope><scope>7TM</scope><scope>K9.</scope><scope>7X8</scope></search><sort><creationdate>20180115</creationdate><title>Live‐Cell Protein Sulfonylation Based on Proximity‐driven N‐Sulfonyl Pyridone Chemistry</title><author>Matsuo, Kazuya ; Nishikawa, Yuki ; Masuda, Marie ; Hamachi, Itaru</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c4762-b6f2bb3e20a8a25f6e790c35579c3f53c1dfce05abf911e3ccada0a73fbd14d73</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2018</creationdate><topic>Biosensors</topic><topic>Fluorescence resonance energy transfer</topic><topic>FRET biosensors</topic><topic>intracellular protein labeling</topic><topic>N-sulfonyl pyridones</topic><topic>Proteins</topic><topic>traceless affinity sulfonylation</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Matsuo, Kazuya</creatorcontrib><creatorcontrib>Nishikawa, Yuki</creatorcontrib><creatorcontrib>Masuda, Marie</creatorcontrib><creatorcontrib>Hamachi, Itaru</creatorcontrib><collection>PubMed</collection><collection>CrossRef</collection><collection>Nucleic Acids Abstracts</collection><collection>ProQuest Health & Medical Complete (Alumni)</collection><collection>MEDLINE - Academic</collection><jtitle>Angewandte Chemie International Edition</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Matsuo, Kazuya</au><au>Nishikawa, Yuki</au><au>Masuda, Marie</au><au>Hamachi, Itaru</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Live‐Cell Protein Sulfonylation Based on Proximity‐driven N‐Sulfonyl Pyridone Chemistry</atitle><jtitle>Angewandte Chemie International Edition</jtitle><addtitle>Angew Chem Int Ed Engl</addtitle><date>2018-01-15</date><risdate>2018</risdate><volume>57</volume><issue>3</issue><spage>659</spage><epage>662</epage><pages>659-662</pages><issn>1433-7851</issn><eissn>1521-3773</eissn><abstract>The development of bioorthogonal approaches for labeling of endogenous proteins under the multimolecular crowding conditions of live cells is highly desirable for the analysis and engineering of proteins without using genetic manipulation. N‐Sulfonyl pyridone (SP) is reported as a new reactive group for protein sulfonylation. The ligand‐directed SP chemistry was able to modify not only purified proteins in vitro, but also endogenous ones on the surface of and inside live cells selectively and rapidly, which allowed to convert endogenous proteins to FRET‐based biosensors in situ.
Ligand‐directed N‐sulfonyl pyridone chemistry afforded the specific sulfonylation of endogenous proteins without disturbing their original nature. This chemical strategy allowed the simple conversion of endogenous proteins in live cell habitats into semisynthetic FRET biosensors for the analysis of the dynamic process in protein–ligand (small molecule) interactions.</abstract><cop>Germany</cop><pub>Wiley Subscription Services, Inc</pub><pmid>29193552</pmid><doi>10.1002/anie.201707972</doi><tpages>4</tpages><edition>International ed. in English</edition></addata></record> |
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| source | Wiley Online Library Journals Frontfile Complete |
| subjects | Biosensors Fluorescence resonance energy transfer FRET biosensors intracellular protein labeling N-sulfonyl pyridones Proteins traceless affinity sulfonylation |
| title | Live‐Cell Protein Sulfonylation Based on Proximity‐driven N‐Sulfonyl Pyridone Chemistry |
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