Selective Radical Trifluoromethylation of Native Residues in Proteins

Imiołek, Mateusz; Karunanithy, Gogulan; Ng, Wai-Lung; Baldwin, Andrew J.; Gouverneur, Véronique; Davis, Benjamin G.

doi:10.1021/jacs.7b10230

Cited by 110 publications

(97 citation statements)

References 64 publications

Supporting

Mentioning

Contrasting

Unclassified

Order By: Relevance

“…The radical process is started by the formation a tert ‐butoxyl radical from TBHP and a Cu I species, as described previously , . Oxidation of the trifluoromethanesulfinate anion by the tert ‐butoxyl radical gives a CF 3 radical and SO 2 , which is further oxidized to HSO 4 – , . Also the formation through an oxidized copper species via a single electron transfer has been suggested .…”

Section: Resultsmentioning

confidence: 96%

Cu and Hydroquinone for the Trifluoromethylation of Unprotected Phenols

et al. 2018

View full text Add to dashboard Cite

Fluorination and trifluoromethylation are indispensable tools in the preparation of modern pharmaceuticals and APIs. Herein we present a concept for the introduction of a trifluoromethyl group into unprotected phenols employing catalytic copper(I) iodide and hydroquinone, t BuOOH, and the Langlois' reagent. The method proceeds under mild conditions and exhibits an extended substrate scope compared to the biocatalytic trifluoromethylation using laccase from Agaricus bisporus . Various functional groups such as aldehydes, esters, ethers, ketones and nitriles were tolerated. The hydroquinone‐mediated trifluoromethylation reaction allowed accessing trifluoromethylated phenols, which are cumbersome to prepare via previously known chemical methods.

show abstract

Section: Resultsmentioning

confidence: 96%

Cu and Hydroquinone for the Trifluoromethylation of Unprotected Phenols

et al. 2018

View full text Add to dashboard Cite

show abstract

“…When applied to membrane proteins, the observed modifications are localized on extramembrane regions, thus demonstrating its aqueous accessibility and compatibility with detergent milieu. Subsequently, the groups of Davis and Krska incubated the Langlois reagent with tert ‐butylhydroperoxide (TBHP) to form . CF 3 for peptide or protein engineering.…”

Section: Applications In Protein Footprintingmentioning

confidence: 99%

The Application of Fluorine‐Containing Reagents in Structural Proteomics

2020

View full text Add to dashboard Cite

Structural proteomics refers to large‐scale mapping of protein structures in order to understand the relationship between protein sequence, structure, and function. Chemical labeling, in combination with mass‐spectrometry (MS) analysis, have emerged as powerful tools to enable a broad range of biological applications in structural proteomics. The key to success is a biocompatible reagent that modifies a protein without affecting its high‐order structure. Fluorine, well‐known to exert profound effects on the physical and chemical properties of reagents, should have an impact on structural proteomics. In this Minireview, we describe several fluorine‐containing reagents that can be applied in structural proteomics. We organize their applications around four MS‐based techniques: a) affinity labeling, b) activity‐based protein profiling (ABPP), c) protein footprinting, and d) protein cross‐linking. Our aim is to provide an overview of the research, development, and application of fluorine‐containing reagents in protein structural studies.

show abstract

“…Für Membranproteine sind die Modifikationen an den Extramembranregionen lokalisiert, was die Wasserzugänglichkeit und Kompatibilität mit dem Detergenzmilieu widerspiegelt. Im Anschluss an diese Arbeit zeigten die Gruppen von Davis und Krska, dass das Langlois‐Reagenz mit t ‐Butylhydroperoxid (TBHP) inkubiert werden kann, um . CF 3 zum Peptid‐ oder Protein‐Engineering zu erzeugen.…”

Section: Anwendungen Im Protein‐footprintingunclassified

Fluorierte Reagenzien in der Strukturproteomik

2020

View full text Add to dashboard Cite

Das Gebiet der Strukturproteomik befasst sich mit der umfassenden Kartierung von Proteinstrukturen, mit dem Ziel, die Beziehung zwischen Proteinsequenz, ‐struktur und ‐funktion zu verstehen. Die Kombination aus chemischer Markierung und Massenspektrometrie‐Analytik hat sich zu einem beliebten Ansatz für biologische Fragestellungen in der Strukturproteomik entwickelt. Hierbei sind biokompatible Reagenzien, die Proteine modifizieren, ohne deren höhere Ordnung zu beeinflussen, der Schlüssel zum Erfolg. Fluor ist bestens dafür bekannt, die physikochemischen Eigenschaften von Reagenzien zu verändern, und spielt daher in der Strukturproteomik eine immer bedeutendere Rolle. In diesem Kurzaufsatz beschreiben wir die Verwendung fluorierter Reagenzien im Bereich der Strukturproteomik. Dabei beziehen wir uns auf MS‐basierte Techniken: a) Affinitätsmarkierung b) Aktivitäts‐basiertes Protein‐Profiling (ABPP), c) Protein‐Footprinting sowie d) Protein‐Crosslinking. Unser Ziel ist es, den Stand der Forschung sowie die Entwicklungen und Anwendungen von fluorierten Reagenzien in der Proteinstrukturanalytik zusammenzufassen.

show abstract

Selective Radical Trifluoromethylation of Native Residues in Proteins

Cited by 110 publications

References 64 publications

Cu and Hydroquinone for the Trifluoromethylation of Unprotected Phenols

Cu and Hydroquinone for the Trifluoromethylation of Unprotected Phenols

The Application of Fluorine‐Containing Reagents in Structural Proteomics

Fluorierte Reagenzien in der Strukturproteomik

Contact Info

Product

Resources

About