Abstract：
Herein we have investigated the formation and interplay of several noncovalent interactions (NCIs) involved in the inhibition of human monoamine oxidase B (MAO B). Concretely, an inspection of the Protein Data Bank (PDB) revealed the formation of a halogen bond (HlgB) between a diphenylene iodonium (DPI) inhibitor and a water molecule present in the active site, in addition to a noncovalent network of interactions (e. g. lone pair-π, hydrogen bonding, OH-π, CH-π and π-stacking interactions) with surrounding protein residues. Several theoretical models were built to understand the strength and directionality features of the HlgB in addition to the interplay with other NCIs present in the active site of the enzyme. Besides, a computational study was carried out using DPI as HlgB donor and several electron rich molecules (CO, H2O, CH2O, HCN, pyridine, OCN-, SCN-, Cl- and Br-) as HlgB acceptors. The results were analyzed using several state-of-the-art computational tools. We expect that our results will be useful for those scientists working in the fields of rational drug design, chemical biology as well as supramolecular chemistry.
摘要：
在本文中，我们研究了与抑制人单胺氧化酶B（MAOB）有关的几种非共价相互作用（NCI）的形成和相互作用。具体而言,对蛋白质数据库（PDB）的检查显示，在二亚苯基碘鎓（DPI）抑制剂和活性位点中存在的水分子之间形成了卤素键（HlgB），除了相互作用的非共价网络(例如孤对子-π，氢键,OH-π,CH-π和π堆叠相互作用）与周围的蛋白质残基。除了与酶活性位点中存在的其他NCI的相互作用外，还建立了几种理论模型来了解HlgB的强度和方向性特征。此外,使用DPI作为HlgB供体和几个富电子分子(CO，H2O,CH2O,HCN,吡啶,OCN-,SCN-,Cl-和Br-)作为HlgB受体。使用几种最先进的计算工具对结果进行了分析。我们希望我们的结果将对那些在合理药物设计领域工作的科学家有用，化学生物学以及超分子化学。
