84359-16-0Relevant academic research and scientific papers
Synthesis of cobalt nanoparticles by pyrolysis of Vitamin B12: A non-noble-metal catalyst for efficient hydrogenation of nitriles
Ferraccioli, Raffaella,Borovika, Diana,Surkus, Annette-Enrica,Kreyenschulte, Carsten,Topf, Christoph,Beller, Matthias
, p. 499 - 507 (2018/02/07)
A facile preparation of vitamin B12-derived carbonaceous cobalt particles supported on ceria is reported. The resulting composite material is obtained upon wet impregnation of ceria with natural cyanocobalamin and consecutive pyrolysis under inert conditions. The novel catalyst shows good to excellent performance in the industrially relevant heterogeneous hydrogenation of nitriles to the corresponding primary amines.
Surface plasmon resonance biosensor based fragment screening using acetylcholine binding protein identifies ligand efficiency hot spots (le hot spots) by deconstruction of nicotinic acetylcholine receptor α7 ligands
De Kloe, Gerdien E.,Retra, Kim,Geitmann, Matthis,K?llblad, Per,Nahar, Tariq,Van Elk, René,Smit, August B.,Van Muijlwijk-Koezen, Jacqueline E.,Leurs, Rob,Irth, Hubertus,Danielson, U. Helena,De Esch, Iwan J. P.
experimental part, p. 7192 - 7201 (2010/12/18)
The soluble acetylcholine binding protein (AChBP) is a homologue of the ligand-binding domain of the nicotinic acetylcholine receptors (nAChR). To guide future fragment-screening using surface plasmon resonance (SPR) biosensor technology as a label-free, direct binding, biophysical screening assay, a focused fragment library was generated based on deconstruction of a set of α7 nAChR selective quinuclidine containing ligands with nanomolar affinities. The interaction characteristics of the fragments and the parent compounds with AChBP were evaluated using an SPR biosensor assay. The data obtained from this direct binding assay correlated well with data from the reference radioligand displacement assay. Ligand efficiencies for different (structural) groups of fragments in the library were correlated to binding with distinct regions of the binding pocket, thereby identifying ligand efficiency hot spots (LE hot spots). These hot spots can be used to identity the most promising hit fragments in a large scale fragment library screen.
Factor Xa inhibitors
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, (2008/06/13)
The invention provides compounds which specifically inhibit factor Xa activity having the structure A1—A2—(A3)m—B, where m is 0 or 1. A compound of the invention is characterized, in part, in that it exhibits a specific inhibition of factor Xa activity with a Ki≦100 μM, preferably ≦2 nM, and does not substantially inhibit the activity of other proteases involved in the coagulation cascade. The invention further provides methods of specifically inhibiting the activity of factor Xa and of inhibiting blood clotting in vitro and in an individual and methods of detecting factor Xa levels or activity.
