Magnetic Resonance Center (CERM), University of Florence, and Interuniversity Consortium for Magnetic Resonance of Metalloproteins (CIRMMP) , Via L. Sacconi 6, 50019 Sesto Fiorentino (FI), Italy.
Department of Chemistry "Ugo Schiff", University of Florence , Via della Lastruccia 3, 50019 Sesto Fiorentino (FI), Italy.
J Phys Chem B. 2017 Aug 31;121(34):8094-8101. doi: 10.1021/acs.jpcb.7b05679. Epub 2017 Aug 16.
Solid-state NMR is becoming a powerful tool to detect atomic-level structural features of biomolecules even when they are bound to (or trapped in) solid systems that lack long-range three-dimensional order. We here demonstrate that it is possible to probe protein-ligand interactions from a protein-based perspective also when the protein is entrapped in silica, thus translating into biomolecular solid-state NMR all of the considerations that are usually made to understand the chemical nature of the interaction of a protein with its ligands. This work provides a proof of concept that also immobilized enzymes can be used for protein-based NMR protein-ligand interactions for drug discovery.
固态 NMR 正在成为一种强大的工具，即使在缺乏长程三维有序的结合（或被困在）固态系统中，也可以检测生物分子的原子级结构特征。我们在这里证明，即使蛋白质被困在二氧化硅中，也可以从基于蛋白质的角度探测蛋白质-配体相互作用，从而将通常用于理解蛋白质与其配体相互作用的化学性质的所有考虑因素转化为生物分子固态 NMR。这项工作提供了一个概念验证，即固定化酶也可以用于基于蛋白质的 NMR 蛋白质-配体相互作用的药物发现。
