193152-96-4Relevant academic research and scientific papers
Diastereoselective alkylation of β-amino esters: Structural and rate studies reveal alkylations of hexameric lithium enolates
McNeil, Anne J.,Toombes, Gilman E. S.,Gruner, Sol M.,Lobkovsky, Emil,Collum, David B.,Chandramouli, Sithamalli V.,Vanasse, Benoit J.,Ayers, Timothy A.
, p. 16559 - 16568 (2004)
Alkylation of β-amino ester enolates proceeds with high diastereoselectivity. Single crystal, powder, and solution X-ray diffraction studies of the enolate show that the racemic enolate forms prismatic hexamers. 6Li NMR spectroscopic studies on partially racemic enolates reveal complex mixtures of homo- and heterochiral hexamers. An implicit fit of the aggregate populations to the Boltzmann distribution provides the free energy differences and equilibrium constants for the ensemble. Rate studies show that enolate alkylation occurs directly from the hexamer with participation by THF. A mechanism based on the alkylation of a ladder-like aggregate is proposed.
Novel crystalline forms of a factor Xa inhibitor
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Page 10-11, (2010/02/05)
The present invention relates to novel crystalline forms of an inhibitor of Factor Xa, processes for its preparation, compositions comprising it, and its therapeutic use.
Optimization of the β-aminoester class of factor Xa inhibitors. Part 1: P4 and side-chain modifications for improved in vitro potency
Czekaj, Mark,Klein, Scott I.,Guertin, Kevin R.,Gardner, Charles J.,Zulli, Allison L.,Pauls, Henry W.,Spada, Alfred P.,Cheney, Daniel L.,Brown, Karen D.,Colussi, Dennis J.,Chu, Valeria,Leadley, Robert J.,Dunwiddie, Christopher T.
, p. 1667 - 1670 (2007/10/03)
A systematic modification of the C3 side-chain of the β-aminoester class of factor Xa inhibitors and a survey of P4 variations is described. These changes have resulted in the identification of sub-nanomolar inhibitors with improved selectivity versus related proteases. Coagulation parameters (i.e., APTT doubling concentrations) are also improved.
