Name
Abstract | ||
|---|---|---|
A docking protocol aimed at obtaining a consistent qualitative and quantitative picture of binding for a series of hERG channel blockers is presented. To overcome the limitations experienced by standard procedures when docking blockers at hERG binding site, we designed a strategy that explicitly takes into account the conformations of the channel, their possible intrinsic symmetry, and the role played by the configurational entropy of ligands. The protocol was developed on a series of congeneric sertindole derivatives, allowing us to satisfactorily explain the structure-activity relationships for this set of blockers. In addition, we show that the performance of structure-based models relying on multiple-receptor conformations statistically increases when the protein conformations are chosen in such a way as to capture relevant structural features at the binding site. The protocol was then successfully applied to a series of structurally unrelated blockers. |
Year | DOI | Venue |
|---|---|---|
2013 | 10.1021/ci300326d | JOURNAL OF CHEMICAL INFORMATION AND MODELING |
DocType | Volume | Issue |
Journal | 53 | 1 |
ISSN | Citations | PageRank |
1549-9596 | 0 | 0.34 |
References | Authors | |
0 | 5 | |
Name | Order | Citations | PageRank |
|---|---|---|---|
| Giovanni Paolo Di Martino | 1 | 0 | 0.34 |
| Matteo Masetti | 2 | 2 | 3.45 |
| Luisa Ceccarini | 3 | 0 | 0.34 |
| Andrea Cavalli | 4 | 11 | 2.39 |
| Maurizio Recanatini | 5 | 18 | 6.57 |