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Luciferase‐Induced Photouncaging: Bioluminolysis
Bioluminescence resonance energy transfer (BRET) has been widely used for studying dynamic processes in biological systems such as protein–protein interactions and other signaling events. Aside from acting as a reporter, BRET can also turn on functions in living systems. Herein, we report the applic...
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| Published in: | Angewandte Chemie International Edition 2019-11, Vol.58 (45), p.16033-16037 |
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| Main Authors: | , , , , , |
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| cites | cdi_FETCH-LOGICAL-c4504-193dffc28aeace7d4feb9cc6eae5860aaaa6399ce660e170de8df82b4652319e3 |
| container_end_page | 16037 |
| container_issue | 45 |
| container_start_page | 16033 |
| container_title | Angewandte Chemie International Edition |
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| creator | Chang, Dalu Lindberg, Eric Feng, Suihan Angerani, Simona Riezman, Howard Winssinger, Nicolas |
| description | Bioluminescence resonance energy transfer (BRET) has been widely used for studying dynamic processes in biological systems such as protein–protein interactions and other signaling events. Aside from acting as a reporter, BRET can also turn on functions in living systems. Herein, we report the application of BRET to performing a biorthogonal reaction in living cells; namely, releasing functional molecules through energy transfer to a coumarin molecule, a process termed bioluminolysis. An efficient BRET from Nanoluc‐Halotag chimera protein (H‐Luc) to a coumarin substrate yields the excited state of coumarin, which in turn triggers hydrolysis to uncage a target molecule. Compared to the conventional methods, this novel uncaging system requires no external light source and shows fast kinetics (t1/2 |
| doi_str_mv | 10.1002/anie.201907734 |
| format | article |
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Let there be light! The unmasking of coumarin‐caged molecules was achieved by a resonance energy transfer (BRET) from a luciferase. The reaction was shown to proceed quickly (t1/2<2 min) in the presence of the luciferase substrate.</description><edition>International ed. in English</edition><identifier>ISSN: 1433-7851</identifier><identifier>EISSN: 1521-3773</identifier><identifier>DOI: 10.1002/anie.201907734</identifier><identifier>PMID: 31478317</identifier><language>eng</language><publisher>Germany: Wiley Subscription Services, Inc</publisher><subject>Biological activity ; Bioluminescence ; BRET ; Cells (biology) ; Coumarin ; Coumarins - metabolism ; Energy transfer ; Enzyme inhibitors ; Fluorescence Resonance Energy Transfer - methods ; halotag ; HeLa Cells ; Humans ; Kinases ; Light sources ; luciferase ; Luciferases - metabolism ; Luminescent Measurements - methods ; Luminescent Proteins - metabolism ; optochemical reactions ; Protein Binding ; Protein interaction ; Proteins ; Pyrazoles - metabolism ; Pyrimidines - metabolism ; Reaction kinetics ; Substrates ; uncaging reactions</subject><ispartof>Angewandte Chemie International Edition, 2019-11, Vol.58 (45), p.16033-16037</ispartof><rights>2019 Wiley‐VCH Verlag GmbH & Co. KGaA, Weinheim</rights><rights>2019 Wiley-VCH Verlag GmbH & Co. KGaA, Weinheim.</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c4504-193dffc28aeace7d4feb9cc6eae5860aaaa6399ce660e170de8df82b4652319e3</citedby><cites>FETCH-LOGICAL-c4504-193dffc28aeace7d4feb9cc6eae5860aaaa6399ce660e170de8df82b4652319e3</cites><orcidid>0000-0002-9245-5576 ; 0000-0002-4258-5583 ; 0000-0003-2006-539X ; 0000-0003-4680-9422 ; 0000-0002-9205-0050 ; 0000-0003-1636-7766</orcidid></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><link.rule.ids>314,777,781,27905,27906</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/31478317$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Chang, Dalu</creatorcontrib><creatorcontrib>Lindberg, Eric</creatorcontrib><creatorcontrib>Feng, Suihan</creatorcontrib><creatorcontrib>Angerani, Simona</creatorcontrib><creatorcontrib>Riezman, Howard</creatorcontrib><creatorcontrib>Winssinger, Nicolas</creatorcontrib><title>Luciferase‐Induced Photouncaging: Bioluminolysis</title><title>Angewandte Chemie International Edition</title><addtitle>Angew Chem Int Ed Engl</addtitle><description>Bioluminescence resonance energy transfer (BRET) has been widely used for studying dynamic processes in biological systems such as protein–protein interactions and other signaling events. Aside from acting as a reporter, BRET can also turn on functions in living systems. Herein, we report the application of BRET to performing a biorthogonal reaction in living cells; namely, releasing functional molecules through energy transfer to a coumarin molecule, a process termed bioluminolysis. An efficient BRET from Nanoluc‐Halotag chimera protein (H‐Luc) to a coumarin substrate yields the excited state of coumarin, which in turn triggers hydrolysis to uncage a target molecule. Compared to the conventional methods, this novel uncaging system requires no external light source and shows fast kinetics (t1/2<2 min). We applied this BRET uncaging system to release a potent kinase inhibitor, ibrutinib, in living cells, highlighting its broad utility in controlling the supply of bioactive small molecules in vivo.
Let there be light! The unmasking of coumarin‐caged molecules was achieved by a resonance energy transfer (BRET) from a luciferase. The reaction was shown to proceed quickly (t1/2<2 min) in the presence of the luciferase substrate.</description><subject>Biological activity</subject><subject>Bioluminescence</subject><subject>BRET</subject><subject>Cells (biology)</subject><subject>Coumarin</subject><subject>Coumarins - metabolism</subject><subject>Energy transfer</subject><subject>Enzyme inhibitors</subject><subject>Fluorescence Resonance Energy Transfer - methods</subject><subject>halotag</subject><subject>HeLa Cells</subject><subject>Humans</subject><subject>Kinases</subject><subject>Light sources</subject><subject>luciferase</subject><subject>Luciferases - metabolism</subject><subject>Luminescent Measurements - methods</subject><subject>Luminescent Proteins - metabolism</subject><subject>optochemical reactions</subject><subject>Protein Binding</subject><subject>Protein interaction</subject><subject>Proteins</subject><subject>Pyrazoles - metabolism</subject><subject>Pyrimidines - metabolism</subject><subject>Reaction kinetics</subject><subject>Substrates</subject><subject>uncaging reactions</subject><issn>1433-7851</issn><issn>1521-3773</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2019</creationdate><recordtype>article</recordtype><recordid>eNqFkL9OwzAQhy0EoqWwMqJKLCwp_pPENlupClSqgAFmy3UuxVUSl7gW6sYj8Iw8Ca5aQGLBy_mk7366-xA6JXhAMKaXurEwoJhIzDlL91CXZJQkLDb78Z8ylnCRkQ468n4ReSFwfog6jKRcMMK7iE6DsSW02sPn-8ekKYKBov_44lYuNEbPbTO_6l9bV4XaNq5ae-uP0UGpKw8nu9pDzzfjp9FdMn24nYyG08SkGU4TIllRloYKDdoAL9ISZtKYHDRkIsc6vpxJaSDPMRCOCxBFKegszTPKiATWQxfb3GXrXgP4laqtN1BVugEXvKJUMClkPDii53_QhQttE7dTlGGRUswJj9RgS5nWed9CqZatrXW7VgSrjU21sal-bMaBs11smNVQ_ODf-iIgt8CbrWD9T5wa3k_Gv-FfVJuB1w</recordid><startdate>20191104</startdate><enddate>20191104</enddate><creator>Chang, Dalu</creator><creator>Lindberg, Eric</creator><creator>Feng, Suihan</creator><creator>Angerani, Simona</creator><creator>Riezman, Howard</creator><creator>Winssinger, Nicolas</creator><general>Wiley Subscription Services, Inc</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>7TM</scope><scope>K9.</scope><scope>7X8</scope><orcidid>https://orcid.org/0000-0002-9245-5576</orcidid><orcidid>https://orcid.org/0000-0002-4258-5583</orcidid><orcidid>https://orcid.org/0000-0003-2006-539X</orcidid><orcidid>https://orcid.org/0000-0003-4680-9422</orcidid><orcidid>https://orcid.org/0000-0002-9205-0050</orcidid><orcidid>https://orcid.org/0000-0003-1636-7766</orcidid></search><sort><creationdate>20191104</creationdate><title>Luciferase‐Induced Photouncaging: Bioluminolysis</title><author>Chang, Dalu ; Lindberg, Eric ; Feng, Suihan ; Angerani, Simona ; Riezman, Howard ; Winssinger, Nicolas</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c4504-193dffc28aeace7d4feb9cc6eae5860aaaa6399ce660e170de8df82b4652319e3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2019</creationdate><topic>Biological activity</topic><topic>Bioluminescence</topic><topic>BRET</topic><topic>Cells (biology)</topic><topic>Coumarin</topic><topic>Coumarins - metabolism</topic><topic>Energy transfer</topic><topic>Enzyme inhibitors</topic><topic>Fluorescence Resonance Energy Transfer - methods</topic><topic>halotag</topic><topic>HeLa Cells</topic><topic>Humans</topic><topic>Kinases</topic><topic>Light sources</topic><topic>luciferase</topic><topic>Luciferases - metabolism</topic><topic>Luminescent Measurements - methods</topic><topic>Luminescent Proteins - metabolism</topic><topic>optochemical reactions</topic><topic>Protein Binding</topic><topic>Protein interaction</topic><topic>Proteins</topic><topic>Pyrazoles - metabolism</topic><topic>Pyrimidines - metabolism</topic><topic>Reaction kinetics</topic><topic>Substrates</topic><topic>uncaging reactions</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Chang, Dalu</creatorcontrib><creatorcontrib>Lindberg, Eric</creatorcontrib><creatorcontrib>Feng, Suihan</creatorcontrib><creatorcontrib>Angerani, Simona</creatorcontrib><creatorcontrib>Riezman, Howard</creatorcontrib><creatorcontrib>Winssinger, Nicolas</creatorcontrib><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><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>Chang, Dalu</au><au>Lindberg, Eric</au><au>Feng, Suihan</au><au>Angerani, Simona</au><au>Riezman, Howard</au><au>Winssinger, Nicolas</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Luciferase‐Induced Photouncaging: Bioluminolysis</atitle><jtitle>Angewandte Chemie International Edition</jtitle><addtitle>Angew Chem Int Ed Engl</addtitle><date>2019-11-04</date><risdate>2019</risdate><volume>58</volume><issue>45</issue><spage>16033</spage><epage>16037</epage><pages>16033-16037</pages><issn>1433-7851</issn><eissn>1521-3773</eissn><abstract>Bioluminescence resonance energy transfer (BRET) has been widely used for studying dynamic processes in biological systems such as protein–protein interactions and other signaling events. 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Let there be light! The unmasking of coumarin‐caged molecules was achieved by a resonance energy transfer (BRET) from a luciferase. The reaction was shown to proceed quickly (t1/2<2 min) in the presence of the luciferase substrate.</abstract><cop>Germany</cop><pub>Wiley Subscription Services, Inc</pub><pmid>31478317</pmid><doi>10.1002/anie.201907734</doi><tpages>5</tpages><edition>International ed. in English</edition><orcidid>https://orcid.org/0000-0002-9245-5576</orcidid><orcidid>https://orcid.org/0000-0002-4258-5583</orcidid><orcidid>https://orcid.org/0000-0003-2006-539X</orcidid><orcidid>https://orcid.org/0000-0003-4680-9422</orcidid><orcidid>https://orcid.org/0000-0002-9205-0050</orcidid><orcidid>https://orcid.org/0000-0003-1636-7766</orcidid><oa>free_for_read</oa></addata></record> |
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| subjects | Biological activity Bioluminescence BRET Cells (biology) Coumarin Coumarins - metabolism Energy transfer Enzyme inhibitors Fluorescence Resonance Energy Transfer - methods halotag HeLa Cells Humans Kinases Light sources luciferase Luciferases - metabolism Luminescent Measurements - methods Luminescent Proteins - metabolism optochemical reactions Protein Binding Protein interaction Proteins Pyrazoles - metabolism Pyrimidines - metabolism Reaction kinetics Substrates uncaging reactions |
| title | Luciferase‐Induced Photouncaging: Bioluminolysis |
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