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Optimisation of the P2 pharmacophore in a series of thrombin inhibitors: Ion-dipole interactions with lysine 60G

Ambler, J; Brown, L; Cockcroft, X-L; Grütter, M; Hayler, J; Janus, D; Jones, D; ... Wathey, B; + view all (1999) Optimisation of the P2 pharmacophore in a series of thrombin inhibitors: Ion-dipole interactions with lysine 60G. Bioorganic & Medicinal Chemistry Letters , 9 (9) 1317 - 1322-1317 - 1322. 10.1016/S0960-894X(99)00172-9.

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Abstract

The optimisation of the P2 pharmacophore in a series of thrombin inhibitors is described. The interaction of a number of piperidine P2 functionalities with lysine 60G of thrombin is explored with reference to the crystal structure of inhibitor enzyme complexes. A primary ion-dipole interaction between the terminal P2 side chain group and lysine 60G is evoked to explain the SAR in this series.

Type: Article
Title: Optimisation of the P2 pharmacophore in a series of thrombin inhibitors: Ion-dipole interactions with lysine 60G
DOI: 10.1016/S0960-894X(99)00172-9
Publisher version: http://www.sciencedirect.com/science/article/pii/S...
UCL classification: UCL > Office of the President and Provost
UCL > School of Life and Medical Sciences > VP Health
UCL > School of Life and Medical Sciences > VP Health > Translational Research Office
URI: http://discovery.ucl.ac.uk/id/eprint/1437174
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