1287660-82-5Relevant academic research and scientific papers
Molecular Engineering of Trifunctional Supported Catalysts for the Aerobic Oxidation of Alcohols
Fernandes, Antony E.,Riant, Olivier,Jensen, Klavs F.,Jonas, Alain M.
, p. 11044 - 11048 (2016)
We describe a simple and general method for the preparation and molecular engineering of supported trifunctional catalysts and their application in the representative Cu/TEMPO/NMI-catalyzed aerobic oxidation of benzyl alcohol. The methodology allows in one single step to immobilize, with precise control of surface composition, both pyta, CuI, TEMPO, and NMI sites on azide-functionalized silica particles. To optimize the performance of the heterogeneous trifunctional catalysts, synergistic interactions are finely engineered through modulating the degree of freedom of the imidazole site as well as tuning the relative surface composition, leading to catalysts with an activity significantly superior to the corresponding homogeneous catalytic system.
MERTK DEGRADERS AND USES THEREOF
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Paragraph 00862; 00863, (2020/01/31)
The present invention provides compounds, compositions thereof, and methods of using the same.
Synthetic antibody protein mimics of infliximab by molecular scaffolding on novel CycloTriVeratrilene (CTV) derivatives
Longin, Ond?ej,Hezwani, Mohammed,Van De Langemheen, Helmus,Liskamp, Rob M. J.
, p. 5254 - 5274 (2018/08/04)
Syntheses of novel semi-orthogonally protected CycloTriVeratrilene (CTV) analogues with enhanced water solubility, that is 3 and 4, derived from the previously described CTV scaffold derivative 2 are described here. These scaffolds 2-4 enabled a sequential introduction of three different complementarity determining region (CDR) mimics via Cu(i)-catalysed azide-alkyne cycloaddition towards medium-sized protein mimics denoted as "synthetic antibodies". The highly optimised sequential introduction enabled selective attachment of three different CDR mimics in a one-pot fashion. This approach of obtaining synthetic antibodies, demonstrated by the synthesis of paratope mimics of monoclonal antibody infliximab (Remicade), provided a facile access to a range of (highly) pre-organised molecules bearing three different (cyclic) peptide segments and may find a wide range of applications in the field of protein-protein interaction disruptors as well as in the development of synthetic vaccines or lectin mimics. The prepared synthetic antibodies were tested for their affinity towards tumour necrosis factor alpha using surface plasmon resonance and synthetic antibodies with micromolar affinities were uncovered.
Synthesis of multivalent glycoclusters from 1-thio-β-D-galactose and their inhibitory activity against the β-galactosidase from E. coli
Cagnoni, Alejandro J.,Varela, Oscar,Gouin, Sebastien G.,Kovensky, Jose,Uhrig, Maria Laura
experimental part, p. 3064 - 3077 (2011/06/21)
The synthesis of multivalent glycoclusters, designed to be compatible with biological systems, is reported. A variety of 1-thio-β-d-galactosides linked to a terminal triple bond through oligoethyleneglycol chains of variable lengths has been synthesized. Also, azide-containing oligosaccharide scaffolds were prepared from trehalose, maltose, and maltotriose by direct azidation with NaN3/PPh3/CBr4. Click reaction between the thiogalactoside residues and the azide scaffolds under microwave irradiation afforded a family of glycoclusters containing 1 to 4 residues of 1-thio-β-D-galactose. The yields went from moderate to excellent, depending on the valency of the desired product. Deacetylation with Et 3N/MeOH/H2O led to the final products. Complete characterization of the products was performed by NMR spectroscopy and HR-MS techniques. Their activities as inhibitors of β-galactosidase from E. coli were determined by using the Lineweaver-Burk method. The use of hydrophilic carbohydrate scaffolds for the synthesis of multivalent galactosides represents an interesting approach to improve their pharmacokinetics and bioavailability. In addition, the presence of the thioglycosidic bond will improve their stability in biological fluids.
