The Cover Feature shows interactions of the aminopeptidase inhibitor bestatin with the antimalarial drug target PfA‐M1. The development of inhibitors/drug candidates typically involves understanding the precise molecular details of their interactions with their targets. X‐ray crystallography can reveal the atomic interactions between the two molecules but is a static ‘snapshot’ of the final state and provides no information on the events before, or in indeed after association. Using molecular simulation techniques, we have mapped the route by which bestatin can dissociate from PfA‐M1. This analysis provides important knowledge that may be exploited in the design of new inhibitors/drugs that target PfA‐M1 and the large M1 aminopeptidase superfamily. More information can be found in the Full Paper by Sheena McGowan et al. on page 2504 in Issue 23, 2018 (DOI: 10.1002/cmdc.201800563).

中文翻译：

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封面功能：绘制恶性疟原虫M1氨肽酶PfA-M1的Bestatin抑制途径和动力学图（ChemMedChem 23/2018）

封面特征显示了氨基肽酶抑制剂Bestatin与抗疟药靶标Pf A-M1的相互作用。抑制剂/候选药物的开发通常涉及了解其与靶标相互作用的精确分子细节。X射线晶体学可以揭示两个分子之间的原子相互作用，但它是最终状态的静态“快照”，并且不提供有关缔合之前或之后的事件的信息。使用分子模拟技术，我们绘制了Bestatin可以从Pf A-M1上解离的途径。该分析提供了重要的知识，可在设计针对Pf的新抑制剂/药物时加以利用A‐M1和大型M1氨肽酶超家族。可以在Sheena McGowan等人的《全文》中找到更多信息。就在第23期，2018页2504（：10.1002 / cmdc.201800563 DOI）。