Istituto di Biostrutture e Bioimmagini-CNR, Naples, Italy.
Neurofarba Department, Section of Pharmaceutical and Nutriceutical Sciences, Università degli Studi di Firenze, Sesto Fiorentino, Florence, Italy.
Biochem Biophys Res Commun. 2021 Apr 9;548:217-221. doi: 10.1016/j.bbrc.2021.02.067. Epub 2021 Feb 27.
Up to date alcohols have been scarcely investigated as carbonic anhydrase (CA) inhibitors. To get more insights into the CA inhibition properties of this class of molecules, in this paper, by means of inhibition assays and X-ray crystallographic studies we report a detailed characterization of the CA inhibition properties and the binding mode to human CA II of benzyl alcohol. Results show that, although possessing a very simple scaffold, this molecule acts as a micromolar CA II inhibitor, which anchors to the enzyme active site by means of an H-bond interaction with the zinc bound solvent molecule. Taken together our results clearly indicate primary alcohols as a class of CA inhibitors that deserve to be more investigated.
迄今为止，醇类作为碳酸酐酶 (CA) 抑制剂的研究甚少。为了更深入地了解这一类分子的 CA 抑制特性，本文通过抑制试验和 X 射线晶体学研究，详细表征了苯甲醇对人碳酸酐酶 II 的抑制特性和结合模式。结果表明，尽管具有非常简单的支架，这种分子仍作为一种微摩尔 CA II 抑制剂，通过与锌结合的溶剂分子的氢键相互作用锚定在酶的活性位点上。总之，我们的研究结果清楚地表明，伯醇类是一类值得进一步研究的 CA 抑制剂。
