Synthesis of fluorinated maltose derivatives for monitoring protein interaction by 19F NMR

A novel reporter system, which is applicable to the 19F NMR investigation of protein interactions, is presented. This approach uses 2-F-labeled maltose as a spy ligand to indirectly probe protein–ligand or protein–protein interactions of proteins fused or tagged to the maltose-binding protein (MBP)....
Ausführliche Beschreibung

Gespeichert in:

Autor*in:	Michaela Braitsch [verfasserIn] Hanspeter Kählig [verfasserIn] Georg Kontaxis [verfasserIn] Michael Fischer [verfasserIn] Toshinari Kawada [verfasserIn] Robert Konrat [verfasserIn] Walther Schmid [verfasserIn]

Format:	E-Artikel
Sprache:	Englisch

Erschienen:	2012

Schlagwörter:	fluorination 19F NMR maltose-binding protein (MBP) maltose derivatives protein interaction

Übergeordnetes Werk:	In: Beilstein Journal of Organic Chemistry - Beilstein-Institut, 2005, 8(2012), 1, Seite 448-455
Übergeordnetes Werk:	volume:8 ; year:2012 ; number:1 ; pages:448-455

Links:	Link aufrufen Link aufrufen Link aufrufen Journal toc

DOI / URN:	10.3762/bjoc.8.51

Katalog-ID:	DOAJ001015605

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520			\|a A novel reporter system, which is applicable to the 19F NMR investigation of protein interactions, is presented. This approach uses 2-F-labeled maltose as a spy ligand to indirectly probe protein–ligand or protein–protein interactions of proteins fused or tagged to the maltose-binding protein (MBP). The key feature is the simultaneous NMR observation of both 19F NMR signals of gluco/manno-type-2-F-maltose-isomers; one isomer (α-gluco-type) binds to MBP and senses the protein interaction, and the nonbinding isomers (β-gluco- and/or α/β-manno-type) are utilized as internal references. Moreover, this reporter system was used for relative affinity studies of fluorinated and nonfluorinated carbohydrates to the maltose-binding protein, which were found to be in perfect agreement with published X-ray data. The results of the NMR competition experiments together with the established correlation between 19F chemical shift data and molecular interaction patterns, suggest valuable applications for studies of protein–ligand interaction interfaces.
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allfields	10.3762/bjoc.8.51 doi (DE-627)DOAJ001015605 (DE-599)DOAJ1ad9bd14d0284ac1b98b4f943818ce06 DE-627 ger DE-627 rakwb eng QD241-441 Michaela Braitsch verfasserin aut Synthesis of fluorinated maltose derivatives for monitoring protein interaction by 19F NMR 2012 Text txt rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier A novel reporter system, which is applicable to the 19F NMR investigation of protein interactions, is presented. This approach uses 2-F-labeled maltose as a spy ligand to indirectly probe protein–ligand or protein–protein interactions of proteins fused or tagged to the maltose-binding protein (MBP). The key feature is the simultaneous NMR observation of both 19F NMR signals of gluco/manno-type-2-F-maltose-isomers; one isomer (α-gluco-type) binds to MBP and senses the protein interaction, and the nonbinding isomers (β-gluco- and/or α/β-manno-type) are utilized as internal references. Moreover, this reporter system was used for relative affinity studies of fluorinated and nonfluorinated carbohydrates to the maltose-binding protein, which were found to be in perfect agreement with published X-ray data. The results of the NMR competition experiments together with the established correlation between 19F chemical shift data and molecular interaction patterns, suggest valuable applications for studies of protein–ligand interaction interfaces. fluorination 19F NMR maltose-binding protein (MBP) maltose derivatives protein interaction Science Q Organic chemistry Hanspeter Kählig verfasserin aut Georg Kontaxis verfasserin aut Michael Fischer verfasserin aut Toshinari Kawada verfasserin aut Robert Konrat verfasserin aut Walther Schmid verfasserin aut In Beilstein Journal of Organic Chemistry Beilstein-Institut, 2005 8(2012), 1, Seite 448-455 (DE-627)490226256 (DE-600)2192461-2 18605397 nnns volume:8 year:2012 number:1 pages:448-455 https://doi.org/10.3762/bjoc.8.51 kostenfrei https://doaj.org/article/1ad9bd14d0284ac1b98b4f943818ce06 kostenfrei https://doi.org/10.3762/bjoc.8.51 kostenfrei https://doaj.org/toc/1860-5397 Journal toc kostenfrei GBV_USEFLAG_A SYSFLAG_A GBV_DOAJ GBV_ILN_20 GBV_ILN_22 GBV_ILN_23 GBV_ILN_24 GBV_ILN_31 GBV_ILN_39 GBV_ILN_40 GBV_ILN_60 GBV_ILN_62 GBV_ILN_63 GBV_ILN_65 GBV_ILN_69 GBV_ILN_70 GBV_ILN_73 GBV_ILN_95 GBV_ILN_105 GBV_ILN_110 GBV_ILN_151 GBV_ILN_161 GBV_ILN_170 GBV_ILN_213 GBV_ILN_230 GBV_ILN_267 GBV_ILN_285 GBV_ILN_293 GBV_ILN_602 GBV_ILN_2014 GBV_ILN_4012 GBV_ILN_4037 GBV_ILN_4112 GBV_ILN_4125 GBV_ILN_4126 GBV_ILN_4249 GBV_ILN_4305 GBV_ILN_4306 GBV_ILN_4307 GBV_ILN_4313 GBV_ILN_4322 GBV_ILN_4323 GBV_ILN_4324 GBV_ILN_4325 GBV_ILN_4338 GBV_ILN_4367 GBV_ILN_4700 AR 8 2012 1 448-455
spelling	10.3762/bjoc.8.51 doi (DE-627)DOAJ001015605 (DE-599)DOAJ1ad9bd14d0284ac1b98b4f943818ce06 DE-627 ger DE-627 rakwb eng QD241-441 Michaela Braitsch verfasserin aut Synthesis of fluorinated maltose derivatives for monitoring protein interaction by 19F NMR 2012 Text txt rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier A novel reporter system, which is applicable to the 19F NMR investigation of protein interactions, is presented. This approach uses 2-F-labeled maltose as a spy ligand to indirectly probe protein–ligand or protein–protein interactions of proteins fused or tagged to the maltose-binding protein (MBP). The key feature is the simultaneous NMR observation of both 19F NMR signals of gluco/manno-type-2-F-maltose-isomers; one isomer (α-gluco-type) binds to MBP and senses the protein interaction, and the nonbinding isomers (β-gluco- and/or α/β-manno-type) are utilized as internal references. Moreover, this reporter system was used for relative affinity studies of fluorinated and nonfluorinated carbohydrates to the maltose-binding protein, which were found to be in perfect agreement with published X-ray data. The results of the NMR competition experiments together with the established correlation between 19F chemical shift data and molecular interaction patterns, suggest valuable applications for studies of protein–ligand interaction interfaces. fluorination 19F NMR maltose-binding protein (MBP) maltose derivatives protein interaction Science Q Organic chemistry Hanspeter Kählig verfasserin aut Georg Kontaxis verfasserin aut Michael Fischer verfasserin aut Toshinari Kawada verfasserin aut Robert Konrat verfasserin aut Walther Schmid verfasserin aut In Beilstein Journal of Organic Chemistry Beilstein-Institut, 2005 8(2012), 1, Seite 448-455 (DE-627)490226256 (DE-600)2192461-2 18605397 nnns volume:8 year:2012 number:1 pages:448-455 https://doi.org/10.3762/bjoc.8.51 kostenfrei https://doaj.org/article/1ad9bd14d0284ac1b98b4f943818ce06 kostenfrei https://doi.org/10.3762/bjoc.8.51 kostenfrei https://doaj.org/toc/1860-5397 Journal toc kostenfrei GBV_USEFLAG_A SYSFLAG_A GBV_DOAJ GBV_ILN_20 GBV_ILN_22 GBV_ILN_23 GBV_ILN_24 GBV_ILN_31 GBV_ILN_39 GBV_ILN_40 GBV_ILN_60 GBV_ILN_62 GBV_ILN_63 GBV_ILN_65 GBV_ILN_69 GBV_ILN_70 GBV_ILN_73 GBV_ILN_95 GBV_ILN_105 GBV_ILN_110 GBV_ILN_151 GBV_ILN_161 GBV_ILN_170 GBV_ILN_213 GBV_ILN_230 GBV_ILN_267 GBV_ILN_285 GBV_ILN_293 GBV_ILN_602 GBV_ILN_2014 GBV_ILN_4012 GBV_ILN_4037 GBV_ILN_4112 GBV_ILN_4125 GBV_ILN_4126 GBV_ILN_4249 GBV_ILN_4305 GBV_ILN_4306 GBV_ILN_4307 GBV_ILN_4313 GBV_ILN_4322 GBV_ILN_4323 GBV_ILN_4324 GBV_ILN_4325 GBV_ILN_4338 GBV_ILN_4367 GBV_ILN_4700 AR 8 2012 1 448-455
allfields_unstemmed	10.3762/bjoc.8.51 doi (DE-627)DOAJ001015605 (DE-599)DOAJ1ad9bd14d0284ac1b98b4f943818ce06 DE-627 ger DE-627 rakwb eng QD241-441 Michaela Braitsch verfasserin aut Synthesis of fluorinated maltose derivatives for monitoring protein interaction by 19F NMR 2012 Text txt rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier A novel reporter system, which is applicable to the 19F NMR investigation of protein interactions, is presented. This approach uses 2-F-labeled maltose as a spy ligand to indirectly probe protein–ligand or protein–protein interactions of proteins fused or tagged to the maltose-binding protein (MBP). The key feature is the simultaneous NMR observation of both 19F NMR signals of gluco/manno-type-2-F-maltose-isomers; one isomer (α-gluco-type) binds to MBP and senses the protein interaction, and the nonbinding isomers (β-gluco- and/or α/β-manno-type) are utilized as internal references. Moreover, this reporter system was used for relative affinity studies of fluorinated and nonfluorinated carbohydrates to the maltose-binding protein, which were found to be in perfect agreement with published X-ray data. The results of the NMR competition experiments together with the established correlation between 19F chemical shift data and molecular interaction patterns, suggest valuable applications for studies of protein–ligand interaction interfaces. fluorination 19F NMR maltose-binding protein (MBP) maltose derivatives protein interaction Science Q Organic chemistry Hanspeter Kählig verfasserin aut Georg Kontaxis verfasserin aut Michael Fischer verfasserin aut Toshinari Kawada verfasserin aut Robert Konrat verfasserin aut Walther Schmid verfasserin aut In Beilstein Journal of Organic Chemistry Beilstein-Institut, 2005 8(2012), 1, Seite 448-455 (DE-627)490226256 (DE-600)2192461-2 18605397 nnns volume:8 year:2012 number:1 pages:448-455 https://doi.org/10.3762/bjoc.8.51 kostenfrei https://doaj.org/article/1ad9bd14d0284ac1b98b4f943818ce06 kostenfrei https://doi.org/10.3762/bjoc.8.51 kostenfrei https://doaj.org/toc/1860-5397 Journal toc kostenfrei GBV_USEFLAG_A SYSFLAG_A GBV_DOAJ GBV_ILN_20 GBV_ILN_22 GBV_ILN_23 GBV_ILN_24 GBV_ILN_31 GBV_ILN_39 GBV_ILN_40 GBV_ILN_60 GBV_ILN_62 GBV_ILN_63 GBV_ILN_65 GBV_ILN_69 GBV_ILN_70 GBV_ILN_73 GBV_ILN_95 GBV_ILN_105 GBV_ILN_110 GBV_ILN_151 GBV_ILN_161 GBV_ILN_170 GBV_ILN_213 GBV_ILN_230 GBV_ILN_267 GBV_ILN_285 GBV_ILN_293 GBV_ILN_602 GBV_ILN_2014 GBV_ILN_4012 GBV_ILN_4037 GBV_ILN_4112 GBV_ILN_4125 GBV_ILN_4126 GBV_ILN_4249 GBV_ILN_4305 GBV_ILN_4306 GBV_ILN_4307 GBV_ILN_4313 GBV_ILN_4322 GBV_ILN_4323 GBV_ILN_4324 GBV_ILN_4325 GBV_ILN_4338 GBV_ILN_4367 GBV_ILN_4700 AR 8 2012 1 448-455
allfieldsGer	10.3762/bjoc.8.51 doi (DE-627)DOAJ001015605 (DE-599)DOAJ1ad9bd14d0284ac1b98b4f943818ce06 DE-627 ger DE-627 rakwb eng QD241-441 Michaela Braitsch verfasserin aut Synthesis of fluorinated maltose derivatives for monitoring protein interaction by 19F NMR 2012 Text txt rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier A novel reporter system, which is applicable to the 19F NMR investigation of protein interactions, is presented. This approach uses 2-F-labeled maltose as a spy ligand to indirectly probe protein–ligand or protein–protein interactions of proteins fused or tagged to the maltose-binding protein (MBP). The key feature is the simultaneous NMR observation of both 19F NMR signals of gluco/manno-type-2-F-maltose-isomers; one isomer (α-gluco-type) binds to MBP and senses the protein interaction, and the nonbinding isomers (β-gluco- and/or α/β-manno-type) are utilized as internal references. Moreover, this reporter system was used for relative affinity studies of fluorinated and nonfluorinated carbohydrates to the maltose-binding protein, which were found to be in perfect agreement with published X-ray data. The results of the NMR competition experiments together with the established correlation between 19F chemical shift data and molecular interaction patterns, suggest valuable applications for studies of protein–ligand interaction interfaces. fluorination 19F NMR maltose-binding protein (MBP) maltose derivatives protein interaction Science Q Organic chemistry Hanspeter Kählig verfasserin aut Georg Kontaxis verfasserin aut Michael Fischer verfasserin aut Toshinari Kawada verfasserin aut Robert Konrat verfasserin aut Walther Schmid verfasserin aut In Beilstein Journal of Organic Chemistry Beilstein-Institut, 2005 8(2012), 1, Seite 448-455 (DE-627)490226256 (DE-600)2192461-2 18605397 nnns volume:8 year:2012 number:1 pages:448-455 https://doi.org/10.3762/bjoc.8.51 kostenfrei https://doaj.org/article/1ad9bd14d0284ac1b98b4f943818ce06 kostenfrei https://doi.org/10.3762/bjoc.8.51 kostenfrei https://doaj.org/toc/1860-5397 Journal toc kostenfrei GBV_USEFLAG_A SYSFLAG_A GBV_DOAJ GBV_ILN_20 GBV_ILN_22 GBV_ILN_23 GBV_ILN_24 GBV_ILN_31 GBV_ILN_39 GBV_ILN_40 GBV_ILN_60 GBV_ILN_62 GBV_ILN_63 GBV_ILN_65 GBV_ILN_69 GBV_ILN_70 GBV_ILN_73 GBV_ILN_95 GBV_ILN_105 GBV_ILN_110 GBV_ILN_151 GBV_ILN_161 GBV_ILN_170 GBV_ILN_213 GBV_ILN_230 GBV_ILN_267 GBV_ILN_285 GBV_ILN_293 GBV_ILN_602 GBV_ILN_2014 GBV_ILN_4012 GBV_ILN_4037 GBV_ILN_4112 GBV_ILN_4125 GBV_ILN_4126 GBV_ILN_4249 GBV_ILN_4305 GBV_ILN_4306 GBV_ILN_4307 GBV_ILN_4313 GBV_ILN_4322 GBV_ILN_4323 GBV_ILN_4324 GBV_ILN_4325 GBV_ILN_4338 GBV_ILN_4367 GBV_ILN_4700 AR 8 2012 1 448-455
allfieldsSound	10.3762/bjoc.8.51 doi (DE-627)DOAJ001015605 (DE-599)DOAJ1ad9bd14d0284ac1b98b4f943818ce06 DE-627 ger DE-627 rakwb eng QD241-441 Michaela Braitsch verfasserin aut Synthesis of fluorinated maltose derivatives for monitoring protein interaction by 19F NMR 2012 Text txt rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier A novel reporter system, which is applicable to the 19F NMR investigation of protein interactions, is presented. This approach uses 2-F-labeled maltose as a spy ligand to indirectly probe protein–ligand or protein–protein interactions of proteins fused or tagged to the maltose-binding protein (MBP). The key feature is the simultaneous NMR observation of both 19F NMR signals of gluco/manno-type-2-F-maltose-isomers; one isomer (α-gluco-type) binds to MBP and senses the protein interaction, and the nonbinding isomers (β-gluco- and/or α/β-manno-type) are utilized as internal references. Moreover, this reporter system was used for relative affinity studies of fluorinated and nonfluorinated carbohydrates to the maltose-binding protein, which were found to be in perfect agreement with published X-ray data. The results of the NMR competition experiments together with the established correlation between 19F chemical shift data and molecular interaction patterns, suggest valuable applications for studies of protein–ligand interaction interfaces. fluorination 19F NMR maltose-binding protein (MBP) maltose derivatives protein interaction Science Q Organic chemistry Hanspeter Kählig verfasserin aut Georg Kontaxis verfasserin aut Michael Fischer verfasserin aut Toshinari Kawada verfasserin aut Robert Konrat verfasserin aut Walther Schmid verfasserin aut In Beilstein Journal of Organic Chemistry Beilstein-Institut, 2005 8(2012), 1, Seite 448-455 (DE-627)490226256 (DE-600)2192461-2 18605397 nnns volume:8 year:2012 number:1 pages:448-455 https://doi.org/10.3762/bjoc.8.51 kostenfrei https://doaj.org/article/1ad9bd14d0284ac1b98b4f943818ce06 kostenfrei https://doi.org/10.3762/bjoc.8.51 kostenfrei https://doaj.org/toc/1860-5397 Journal toc kostenfrei GBV_USEFLAG_A SYSFLAG_A GBV_DOAJ GBV_ILN_20 GBV_ILN_22 GBV_ILN_23 GBV_ILN_24 GBV_ILN_31 GBV_ILN_39 GBV_ILN_40 GBV_ILN_60 GBV_ILN_62 GBV_ILN_63 GBV_ILN_65 GBV_ILN_69 GBV_ILN_70 GBV_ILN_73 GBV_ILN_95 GBV_ILN_105 GBV_ILN_110 GBV_ILN_151 GBV_ILN_161 GBV_ILN_170 GBV_ILN_213 GBV_ILN_230 GBV_ILN_267 GBV_ILN_285 GBV_ILN_293 GBV_ILN_602 GBV_ILN_2014 GBV_ILN_4012 GBV_ILN_4037 GBV_ILN_4112 GBV_ILN_4125 GBV_ILN_4126 GBV_ILN_4249 GBV_ILN_4305 GBV_ILN_4306 GBV_ILN_4307 GBV_ILN_4313 GBV_ILN_4322 GBV_ILN_4323 GBV_ILN_4324 GBV_ILN_4325 GBV_ILN_4338 GBV_ILN_4367 GBV_ILN_4700 AR 8 2012 1 448-455
language	English
source	In Beilstein Journal of Organic Chemistry 8(2012), 1, Seite 448-455 volume:8 year:2012 number:1 pages:448-455
sourceStr	In Beilstein Journal of Organic Chemistry 8(2012), 1, Seite 448-455 volume:8 year:2012 number:1 pages:448-455
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topic_facet	fluorination 19F NMR maltose-binding protein (MBP) maltose derivatives protein interaction Science Q Organic chemistry
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container_title	Beilstein Journal of Organic Chemistry
authorswithroles_txt_mv	Michaela Braitsch @@aut@@ Hanspeter Kählig @@aut@@ Georg Kontaxis @@aut@@ Michael Fischer @@aut@@ Toshinari Kawada @@aut@@ Robert Konrat @@aut@@ Walther Schmid @@aut@@
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callnumber-first	Q - Science
author	Michaela Braitsch
spellingShingle	Michaela Braitsch misc QD241-441 misc fluorination misc 19F NMR misc maltose-binding protein (MBP) misc maltose derivatives misc protein interaction misc Science misc Q misc Organic chemistry Synthesis of fluorinated maltose derivatives for monitoring protein interaction by 19F NMR
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topic_title	QD241-441 Synthesis of fluorinated maltose derivatives for monitoring protein interaction by 19F NMR fluorination 19F NMR maltose-binding protein (MBP) maltose derivatives protein interaction
topic	misc QD241-441 misc fluorination misc 19F NMR misc maltose-binding protein (MBP) misc maltose derivatives misc protein interaction misc Science misc Q misc Organic chemistry
topic_unstemmed	misc QD241-441 misc fluorination misc 19F NMR misc maltose-binding protein (MBP) misc maltose derivatives misc protein interaction misc Science misc Q misc Organic chemistry
topic_browse	misc QD241-441 misc fluorination misc 19F NMR misc maltose-binding protein (MBP) misc maltose derivatives misc protein interaction misc Science misc Q misc Organic chemistry
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title	Synthesis of fluorinated maltose derivatives for monitoring protein interaction by 19F NMR
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title_full	Synthesis of fluorinated maltose derivatives for monitoring protein interaction by 19F NMR
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author_browse	Michaela Braitsch Hanspeter Kählig Georg Kontaxis Michael Fischer Toshinari Kawada Robert Konrat Walther Schmid
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title_sort	synthesis of fluorinated maltose derivatives for monitoring protein interaction by 19f nmr
callnumber	QD241-441
title_auth	Synthesis of fluorinated maltose derivatives for monitoring protein interaction by 19F NMR
abstract	A novel reporter system, which is applicable to the 19F NMR investigation of protein interactions, is presented. This approach uses 2-F-labeled maltose as a spy ligand to indirectly probe protein–ligand or protein–protein interactions of proteins fused or tagged to the maltose-binding protein (MBP). The key feature is the simultaneous NMR observation of both 19F NMR signals of gluco/manno-type-2-F-maltose-isomers; one isomer (α-gluco-type) binds to MBP and senses the protein interaction, and the nonbinding isomers (β-gluco- and/or α/β-manno-type) are utilized as internal references. Moreover, this reporter system was used for relative affinity studies of fluorinated and nonfluorinated carbohydrates to the maltose-binding protein, which were found to be in perfect agreement with published X-ray data. The results of the NMR competition experiments together with the established correlation between 19F chemical shift data and molecular interaction patterns, suggest valuable applications for studies of protein–ligand interaction interfaces.
abstractGer	A novel reporter system, which is applicable to the 19F NMR investigation of protein interactions, is presented. This approach uses 2-F-labeled maltose as a spy ligand to indirectly probe protein–ligand or protein–protein interactions of proteins fused or tagged to the maltose-binding protein (MBP). The key feature is the simultaneous NMR observation of both 19F NMR signals of gluco/manno-type-2-F-maltose-isomers; one isomer (α-gluco-type) binds to MBP and senses the protein interaction, and the nonbinding isomers (β-gluco- and/or α/β-manno-type) are utilized as internal references. Moreover, this reporter system was used for relative affinity studies of fluorinated and nonfluorinated carbohydrates to the maltose-binding protein, which were found to be in perfect agreement with published X-ray data. The results of the NMR competition experiments together with the established correlation between 19F chemical shift data and molecular interaction patterns, suggest valuable applications for studies of protein–ligand interaction interfaces.
abstract_unstemmed	A novel reporter system, which is applicable to the 19F NMR investigation of protein interactions, is presented. This approach uses 2-F-labeled maltose as a spy ligand to indirectly probe protein–ligand or protein–protein interactions of proteins fused or tagged to the maltose-binding protein (MBP). The key feature is the simultaneous NMR observation of both 19F NMR signals of gluco/manno-type-2-F-maltose-isomers; one isomer (α-gluco-type) binds to MBP and senses the protein interaction, and the nonbinding isomers (β-gluco- and/or α/β-manno-type) are utilized as internal references. Moreover, this reporter system was used for relative affinity studies of fluorinated and nonfluorinated carbohydrates to the maltose-binding protein, which were found to be in perfect agreement with published X-ray data. The results of the NMR competition experiments together with the established correlation between 19F chemical shift data and molecular interaction patterns, suggest valuable applications for studies of protein–ligand interaction interfaces.
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title_short	Synthesis of fluorinated maltose derivatives for monitoring protein interaction by 19F NMR
url	https://doi.org/10.3762/bjoc.8.51 https://doaj.org/article/1ad9bd14d0284ac1b98b4f943818ce06 https://doaj.org/toc/1860-5397
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author2	Hanspeter Kählig Georg Kontaxis Michael Fischer Toshinari Kawada Robert Konrat Walther Schmid
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Synthesis of fluorinated maltose derivatives for monitoring protein interaction by 19F NMR

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