16365-25-6Relevant articles and documents
Chemoselective hydrosilylation of carboxylic acids using a phosphine-free ruthenium complex and phenylsilane
Abhilash, Vishwanathan,Gadakh, Amol V.,Ganesh, Sambasivam,Hegde, Shivaprasad N.,Jacob, Anand,Karthik, C. S.,Lamees, Thundianandi,Mathivanan, Namachivayam,Sathiyanarayanan, Arumugam Murugan
supporting information, (2022/03/01)
A highly chemoselective hydrosilylation of carboxylic acids was achieved using a bench-stable, phosphine-free Ru-complex tethered with hemi-labile thiophene ligands as the catalyst, employing phenylsilane as the reducing agent. The methodology was further elaborated towards the one-pot synthesis of indole and benzoxazine via tandem reduction/cyclization of acid and nitro group.
METHODS FOR PREPARING FUEL ADDITIVES
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Page/Page column 35, (2019/07/17)
A method is provided for preparing a fuel additive having the formula: ( l ) The method comprises carrying out the following reactions: (i) addition of an alkylating agent b to starting material a: (a) to form an intermediate c; and (ii) ring closing intermediate c to form fuel additive e.
Toward the Rational Design of Galactosylated Glycoclusters That Target Pseudomonas aeruginosa Lectin A (LecA): Influence of Linker Arms That Lead to Low-Nanomolar Multivalent Ligands
Wang, Shuai,Dupin, Lucie,No?l, Mathieu,Carroux, Cindy J.,Renaud, Louis,Géhin, Thomas,Meyer, Albert,Souteyrand, Eliane,Vasseur, Jean-Jacques,Vergoten, Gérard,Chevolot, Yann,Morvan, Fran?ois,Vidal, Sébastien
supporting information, p. 11785 - 11794 (2016/08/05)
Anti-infectious strategies against pathogen infections can be achieved through antiadhesive strategies by using multivalent ligands of bacterial virulence factors. LecA and LecB are lectins of Pseudomonas aeruginosa implicated in biofilm formation. A series of 27 LecA-targeting glycoclusters have been synthesized. Nine aromatic galactose aglycons were investigated with three different linker arms that connect the central mannopyranoside core. A low-nanomolar (Kd=19 nm, microarray) ligand with a tyrosine-based linker arm could be identified in a structure–activity relationship study. Molecular modeling of the glycoclusters bound to the lectin tetramer was also used to rationalize the binding properties observed.