Molecular Simulation Engineering (MOSE) Laboratory - DEA, University of Trieste, Piazzale Europa 1, 34127 Trieste, Italy.
Bioorg Med Chem Lett. 2013 May 15;23(10):2868-71. doi: 10.1016/j.bmcl.2013.03.087. Epub 2013 Mar 30.
The highly selective σ1 receptor antagonist S1RA is endowed with a surprisingly high affinity for its target protein given a missing fundamental hydrophobic pharmacophoric requirement. Here we show that, with respect to other potent σ1 ligands, S1RA is able to compensate this loss by fulfilling all other pharmacophoric requirements and by gaining in solvation energy.
高度选择性的 σ1 受体拮抗剂 S1RA 对其靶蛋白具有惊人的高亲和力，尽管缺少一个基本的疏水药效团要求。在这里，我们表明，与其他强效的 σ1 配体相比，S1RA 能够通过满足所有其他药效团要求并获得溶剂化能来弥补这种损失。
