29389-23-9Relevant academic research and scientific papers
Solid-supported cross-metathesis and a formal alkane metathesis for the generation of biologically relevant molecules
Mndez, Luciana,Mata, Ernesto G.
, p. 81 - 86 (2015/08/18)
Solid-phase synthetic strategies toward the generation of libraries of biologically relevant molecules were developed using olefin cross-metathesis as a key step. It is remarkably the formal alkane metathesis based on a one-pot, microwave-assisted, ruthenium-catalyzed cross-metathesis and reduction to obtain Csp3-Csp3 linkages.
Gold-catalysed cyclic ether formation from diols
Jiang, Xiaolu,London, Emma K.,Morris, David J.,Clarkson, Guy J.,Wills, Martin
supporting information; experimental part, p. 9828 - 9834 (2011/02/23)
Gold(I) and (III) salts have been found to be highly effective at the catalysis of ether formation from alcohols. Intramolecular ether formation of a 1,5-diol was also achieved, with a stereoselectivity that indicates that an SN1 mechanism predominates. In an attempt to form a seven-membered ring, a stable 14-membered dimer product was also formed. Attempts to control the diastereoselectivity of the reaction using a chiral anionic counterion did not give products with a high de.
Novel synthetic inhibitors of selectin-mediated cell adhesion: Synthesis of 1,6-bis[3-(3-carboxymethylphenyl)-4-(2-α-D-mannopyranosyloxy)phenyl] hexane (TBC1269)
Kogan, Timothy P.,Dupré, Brian,Bui, Huong,McAbee, Kathy L.,Kassir, Jamal M.,Scott, Ian L.,Hu, Xin,Vanderslice, Peter,Beck, Pamela J.,Dixon, Richard A. F.
, p. 1099 - 1111 (2007/10/03)
Reports of a high-affinity ligand for E-selectin, sialyl di-Lewis(x) (sLe(x)Le(x), 1), motivated us to incorporate modifications to previously reported biphenyl-based inhibitors that would provide additional interactions with the protein. These compounds were assayed for the ability to inhibit the binding of sialyl Lewis(x) (sLe(x), 2) bearing HL-60 cells to E-, P-, and L- selectin fusion proteins. We report that dimeric or trimeric compounds containing multiple components of simple nonoligosaccharide selectin antagonists inhibit sLe(x)-dependent binding with significantly enhanced potency over the monomeric compound. The enhanced potency is consistent with additional binding interactions within a single selectin lectin domain; however, multivalent interaction with multiple lectin domains as a possible alternative cannot be ruled out. Compound 15e (TBC1269) showed optimal in vitro activity from this class of antagonists and is currently under development for use in the treatment of asthma.
