Tetrabutylammonium Fluoride-Mediated Rapid Alkylation Reaction in Microtiter Plates for the Discovery of Enzyme Inhibitors in Situ

ChemBioChem ◽  
2005 ◽  
Vol 6 (12) ◽  
pp. 2176-2180 ◽  
Author(s):  
Chung-Yi Wu ◽  
Ashraf Brik ◽  
Sheng-Kai Wang ◽  
Yu-Hsien Chen ◽  
Chi-Huey Wong
Keyword(s):  
Enzyme Inhibitors ◽  
Alkylation Reaction ◽  
Microtiter Plates ◽  
Tetrabutylammonium Fluoride

Epoxide opening in water and screening in situ for rapid discovery of enzyme inhibitors in microtiter plates

2006 ◽  
Vol 14 (4) ◽  
pp. 1058-1062 ◽  
Author(s):  
Fu-Sen Liang ◽  
Ashraf Brik ◽  
Ying-Chuan Lin ◽  
John H. Elder ◽  
Chi-Huey Wong
Keyword(s):  
Enzyme Inhibitors ◽  
Microtiter Plates ◽  
Epoxide Opening

scholarly journals A cross-dehydrogenative C(sp3)−H heteroarylation via photo-induced catalytic chlorine radical generation

2021 ◽  
Vol 12 (1) ◽  
Author(s):  
Chia-Yu Huang ◽  
Jianbin Li ◽  
Chao-Jun Li
Keyword(s):  
Hydrogen Atom ◽  
Hydrogen Evolution ◽  
Alkyl Radical ◽  
Cobalt Catalyst ◽  
Alkylation Reaction ◽  
Hydrogen Atom Abstraction ◽  
Dehydrogenative Coupling ◽  
Radical Generation ◽  
Limited Scope

AbstractHydrogen atom abstraction (HAT) from C(sp3)–H bonds of naturally abundant alkanes for alkyl radical generation represents a promising yet underexplored strategy in the alkylation reaction designs since involving stoichiometric oxidants, excessive alkane loading, and limited scope are common drawbacks. Here we report a photo-induced and chemical oxidant-free cross-dehydrogenative coupling (CDC) between alkanes and heteroarenes using catalytic chloride and cobalt catalyst. Couplings of strong C(sp3)–H bond-containing substrates and complex heteroarenes, have been achieved with satisfactory yields. This dual catalytic platform features the in situ engendered chlorine radical for alkyl radical generation and exploits the cobaloxime catalyst to enable the hydrogen evolution for catalytic turnover. The practical value of this protocol was demonstrated by the gram-scale synthesis of alkylated heteroarene with merely 3 equiv. alkane loading.

scholarly journals The Fluoride Anion-Catalyzed Sulfurization of Thioketones with Elemental Sulfur Leading to Sulfur-Rich Heterocycles: First Sulfurization of Thiochalcones

Molecules ◽  
2021 ◽  
Vol 26 (4) ◽  
pp. 822
Author(s):  
Grzegorz Mlostoń ◽  
Jakub Wręczycki ◽  
Katarzyna Urbaniak ◽  
Dariusz M. Bieliński ◽  
Heinz Heimgartner
Keyword(s):  
Elemental Sulfur ◽  
Fluoride Anion ◽  
Ring Size ◽  
Mild Conditions ◽  
Tetrabutylammonium Fluoride ◽  
Cesium Fluoride ◽  
Secondary Reactions ◽  
Derivatives Of

Fluoride anion was demonstrated as a superior activator of elemental sulfur (S8) to perform sulfurization of thioketones leading to diverse sulfur-rich heterocycles. Due to solubility problems, reactions must be carried out either in THF using tetrabutylammonium fluoride (TBAF) or in DMF using cesium fluoride (CsF), respectively. The reactive sulfurizing reagents are in situ generated, nucleophilic fluoropolysulfide anions FS(8−x)−, which react with the C=S bond according to the carbophilic addition mode. Dithiiranes formed thereby, existing in an equilibrium with the ring-opened form (diradicals/zwitterions) are key-intermediates, which undergo either a step-wise dimerization to afford 1,2,4,5-tetrathianes or an intramolecular insertion, leading in the case of thioxo derivatives of 2,2,4,4-tetramethylcyclobutane-1,3-dione to ring enlarged products. In reactions catalyzed by TBAF, water bounded to fluoride anion via H-bridges and forming thereby its stable hydrates is involved in secondary reactions leading, e.g., in the case of 2,2,4,4-tetramethyl-3-thioxocyclobutanone to the formation of some unexpected products such as the ring enlarged dithiolactone and ring-opened dithiocarboxylate. In contrast to thioketones, the fluoride anion catalyzed sulfurization of their α,β-unsaturated analogues, i.e., thiochalcones is slow and inefficient. However, an alternative protocol with triphenylphosphine (PPh3) applied as a catalyst, offers an attractive approach to the synthesis of 3H-1,2-dithioles via 1,5-dipolar electrocyclization of the in situ-generated α,β-unsaturated thiocabonyl S-sulfides. All reactions occur under mild conditions and can be considered as attractive methods for the preparation of sulfur rich heterocycles with diverse ring-size.

Titelbild: In Situ Assembly and Screening of Enzyme Inhibitors with Surface-Tension Microarrays (Angew. Chem. 41/2009)

2009 ◽  
Vol 121 (41) ◽  
pp. 7589-7589
Author(s):  
Laurent Mugherli ◽  
Olga N. Burchak ◽  
Larissa A. Balakireva ◽  
Aline Thomas ◽  
François Chatelain ◽  
...  
Keyword(s):  
Surface Tension ◽  
Enzyme Inhibitors

scholarly journals Development and Validation of a Simple Cell-Based Fluorescence Assay for Dipeptidyl Peptidase 1 (DPP1) Activity

2010 ◽  
Vol 16 (1) ◽  
pp. 36-43 ◽  
Author(s):  
Bob Thong ◽  
James Pilling ◽  
Edward Ainscow ◽  
Raj Beri ◽  
John Unitt
Keyword(s):  
Cell Sorting ◽  
Enzyme Inhibitors ◽  
Dipeptidyl Peptidase ◽  
Fluorescence Assay ◽  
Enzyme Assays ◽  
Fluorogenic Substrates ◽  
Intracellular Degradation ◽  
Dipeptidyl Aminopeptidase ◽  
Development And Validation

Dipeptidyl peptidase 1 (DPP1) (EC 3.4.14.1; also known as cathepsin C, cathepsin J, dipeptidyl aminopeptidase, and dipeptidyl aminotransferase) is a lysosomal cysteinyl protease of the papain family involved in the intracellular degradation of proteins. Isolated enzyme assays for DPP1 activity using a variety of synthetic substrates such as dipeptide or peptide linked to amino-methyl-coumarin (AMC) or other fluorophores are well established. There is, however, no report of a simple whole-cell-based assay for measuring lysosomal DPP1 activity other than the use of flow cytometry (fluorescence-activated cell sorting) or the use of invasive activity-based probes or the production of physiological products such as neutrophil elastase. The authors investigated a number of DPP1 fluorogenic substrates that have the potential to access the lysosome and enable the measurement of DPP1 enzyme activity in situ. They describe the development and evaluation of a simple noninvasive fluorescence assay for measuring DPP1 activity in fresh or cryopreserved human THP-1 cells using the substrate H-Gly-Phe-AFC (amino-fluoro-coumarin). This cell-based fluorescence assay can be performed in a 96-well plate format and is ideally suited for determining the cell potency of potential DPP1 enzyme inhibitors.

In situ assembly of enzyme inhibitors using extended tethering

2003 ◽  
Vol 21 (3) ◽  
pp. 308-314 ◽  
Author(s):  
Daniel A. Erlanson ◽  
Joni W. Lam ◽  
Christian Wiesmann ◽  
Tinh N. Luong ◽  
Robert L. Simmons ◽  
...  
Keyword(s):  
Enzyme Inhibitors

Chiral phosphoric acid catalyzed enantioselective N-alkylation of indoles with in situ generated cyclic N-acyl ketimines

2018 ◽  
Vol 54 (66) ◽  
pp. 9230-9233 ◽  
Author(s):  
Lvye Zhang ◽  
Binqiang Wu ◽  
Zhangtao Chen ◽  
Jinjin Hu ◽  
Xiaofei Zeng ◽  
...  
Keyword(s):  
Phosphoric Acid ◽  
Alkylation Reaction ◽  
Chiral Phosphoric Acid ◽  
Acid Catalyzed

A chiral SPINOL derived phosphoric acid-catalyzed asymmetric N-alkylation reaction of indoles with cyclic α-diaryl-substituted N-acyl imines, which are generated in situ from 3-aryl 3-hydroxyisoindo-linones, has been demonstrated.

In situ reactive compatibilization of PP/ABS blends via Friedel-Crafts alkylation reaction

2015 ◽  
Vol 24 (1) ◽  
pp. 14-24 ◽  
Author(s):  
Parvaneh Eskandari ◽  
Majid Mehrabi Mazidi ◽  
Mir Karim Razavi Aghjeh
Keyword(s):  
Alkylation Reaction ◽  
Reactive Compatibilization

In Situ Click Chemistry:  Enzyme Inhibitors Made to Their Own Specifications

2004 ◽  
Vol 126 (40) ◽  
pp. 12809-12818 ◽  
Author(s):  
Roman Manetsch ◽  
Antoni Krasiński ◽  
Zoran Radić ◽  
Jessica Raushel ◽  
Palmer Taylor ◽  
...  
Keyword(s):  
Click Chemistry ◽  
Enzyme Inhibitors
Sign in / Sign up

Export Citation Format

Share Document